ChemSemBlog

The chemistry seminar that was held on January 28, 2010 was titled “Peptide Design Using Unnatural Amino Acids & Multivalent Antibody Aggregation,” and the speaker was Basar Bilgicer. However, he only presented about multivalent antibody aggregation. Basar Bilgicer was born in Istanbul and received a bachelor’s degree in chemistry at Bogazici University, Turkey. Following that, he received a Ph.D. at Tuff University.

He has studied the thermodynamics and kinetics of multivalent interactions. To be more specific, he studied the association of bivalent antibodies.  He began the presentation by showing the shape of IgG. The Y shape of IgG allows it to easily bind to other molecules. The two arms of this IgG can bind to an antigen since two arms are really flexible.  He used chromatography to separate aggregates based on the size. And then he found out that trimers were the most popular aggregates.

Moreover, although there are a lot of different types of binding, there are two binding types that work best. They are monovalent and bivalent binding; monovalent is binding with one arm and bivalent is binding with two arms. He compared the energy loss between monovalent and bivalent. Since bivalent binds with two arms, we would assume that it would lose twice the amount of monovalent, but surprisingly, it was not. the loss that would be assumed is twice as much as monovalent, however, it was not.

Overall, his presentation was interesting because immunology is the one subject that we can always find in our life. When we get hurt and sick, the body’s reaction can be studied by understanding immunology. Also, he was such a good speaker that we had really good time asking and answering questions.

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The guest speaker of the chemistry seminar held on January 28 was Basar Bilgicer, who is an assistant professor in the Department of Chemical & Biomolecular Engineering at University of Notre Dame. During the presentation, he focused on antibodies, such as IgG, and their aggregations to form multivalent molecules in biological systems and friendly explained about them. I think his seminar really helped students get a deeper understanding of antibody aggregation.

I was very interested in the pathway to make cyclic dimers and trimers from monomers. Bivalent hapten makes it possible to generate several forms of aggregations such as trimer, tetramer, and other polymers. Moreover, depending on the concentration of the ligands that bind to the tips of antibody, more complex form can be produced. For example, a synthetic trivalent hapten, which is monocyclic, aggregates IgG into bicyclic trimers. Through his presentation, I also learned about the thermodynamics and kinetics of multivalent molecules of antibodies, based on the basic dynamic principles. For example, the bicyclic trimer is kinetically and thermodynamically more stable than monomeric aggregates of this IgG.

On the other hand, I have a question about the aggregation of other antibodies rather than IgG antibody that he focused on for his research and about the potential application of antibody aggregates in future biotechnology.

I would say to my ‘non-science’ friends or family that the study of antibody is very important for design of diagnostic molecules for therapy of diseases, and Dr. Bilgicer has worked in multivalent interactions of antibody aggregation in biological systems.

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On January 28, 2010, Basar Bilgicer who is a professor at University of Notre Dame visited Andrews University for his presentation. Mr. Basar Bilgicer prepared two presentations. One of them was “Peptide Design Using Unnatural Amino Acids.” The other was “Multivalent Antibody Aggregation.”  More students in the presentation wanted to know about the antibody aggregation. Therefore, he started the presentation, introducing us the basis of antibody. Especially, he talked about IgG antigen. Overall, he showed us a lot of illustrations which explained how the antibody which has bivalency or trivalency worked with antigens and ligands. Also, he used chromatographic graphs which supported his experimental results. It made me easy to understand how the antibody aggregates in various ways.

There were several kinds of ways which antibody binds to antigen or ligands. Largely, the antigens were divided up depending on the shape, whether they are bivalent, or trivalent. Then, they generated several aggregates, such as dimer, trimer, tetramer, or polymer. They also were produced in a cyclic form, a linear form, or in the middle.

During the presentation, he gave details about the correlation between the Gibbs free energy and the binding constant. I asked him about the effects of temperature on the binding constant. He answered that denaturing occurs above five to ten Celsius degree than the body temperature and the binding constant decreases as the temperature decreases under room temperature.

I would tell my friends that the presentation was about the kind of how and what is involved in binding between antibodies and antigens, or ligands.

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On January 25^th our chem seminar speaker traveled ALL the way from South Bend, IN to give us a very informative lecture on how unnatural amino acids & multivalent antibody aggregation is crucial to science research. Our presenter was Başar Bilgiçer, assistant professor in both the Chemical and Bimolecular Engineering Department and the Chemistry and Biochemistry Department at the University of Notre Dame. He completed his B.S. in Chemistry at Bogazici University, Turkey; he then went on to receive his Ph.D. in chemistry at Tufts University. Bilgiçer conducted his Postdoctoral Fellow at Harvard University.  Dr. Bilgiçer seemed very comfortable and relaxed during his presentation; he was very easy to follow and did a great job at explaining his research so that we could understand it.

The essence of Bilgiçer’s talk was multivalent antibodies and how important the number of bonds to its antigen is in eliciting an immune response to expel the foreign pathogen. In biology class we learn that anything that triggers an immune response is an antigen. When an antigen enters the body, antibodies attach to it forming an antibody-antigen complex that signals the immune system to come and destroy the invading substance. However the efficiency of this system is dependent upon several things, one of which is the valence of the responding antibody.

Antibodies can either be Monovalent or divalent. Bilgiçer easily explained the difference between the two by comparing the arms of the antibody to human body arms. If you are pulling something with your arms it is a lot easier to hold on to it with two arms than with one, this is the same concept with antibodies holding on to antigens. An antibody can hang on to an antigen better when both “arms” of the antibody are attached; this creates bonds that are stronger and tighter; therefore it is harder for the antigen to escape and an immune response can quickly be initiated.

Although this may seem thermodynamically unfavorable, surprising Bilgiçer discovered that it wasn’t; in fact, the entropy decrease for monvalent and divalent antibodies was equitant. This is because whether the antibody bonds with one “arm” or two they would occur that the same time. The multivalent nature of antibodies is advantages in that currently most drugs containing antibodies are monovalent, thus we can create more effective drugs by applying multivalent properties to these antibodies.

Overall I really enjoyed this presentation the only question I have left are: 1. I thought Immune response amplification corresponds with signaling molecules, and so although divalent molecules can hold on better, does the decrease in available antibody binding sites decrease the signal amplification?  2. Most of the antibody aggregates formed very complex arrangements; however, can all of the aggregates bind to the antibody? will a single molecule be just as efficient?  3. If these antibodies are able to elicit a better immune response will lower medicine dosages be required?

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This week in Chemistry Seminar we enjoyed a presentation from Dr. Basar Bilgicer on the aggregation of antibodies and their “antigens” with each other. First of all, a quick recap on antibodies, what they are, what they are used for, and why they are so critical. Antibodies are proteins produced by cells of the immune system and, when bound to their specific antigen (toxin, carcinogen, etc.) will elicit an immune response to increase the number of antibodies in the blood. Antibodies, therefore, are nothing more than a traveling active site for toxins and unwanted stimuli. Instead of bringing about the harm they would typically cause, the antibody-antigen complex is recognized by cells of the immune system and pump out additional antibodies to quell the invasion of toxins. These now harmless macromolecules are then disposed of.

Dr. Bilgicer’s research was in the field of antibody aggregation using substrates acting as two different substrates. During the course of his research, he used size-exclusion chromatography to separate aggregates based on the size of the aggregate. He found that many of the aggregates identified were trimers consisting of three antibodies and three substrates bound partly to one antibody and partly to its adjacent partner. Dr. Bilgicer’s research supports this as the major product of antibody aggregation.

Dr. Bilgicer took some time warming up to the class, but he was competent and knowledgeable in his field. He’s done additional work with more natural substrates for antibodies as well. Although the substrates used in his current experiment are unnatural, the aggregation pattern should not be altered. I found this seminar to helpful in that it provided good explanations of antibody function, including the disabling of the myth that toxins are bound to the crux of the antibody instead of the end of its two prominent limbs. I thought Dr. Bilgicer could have gone into more detail, however, into the main differences between natural and unnatural substrates or into the effects of a natural solution on antibody aggregation.

To the layperson, this seminar was about one way in which the body voids itself of poisons, and how those poisons are organized after they are “caught.”

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This week’s speaker was Basar Bilgicer, who presented on multivalent antibodies.  He stated that one of the major challenges for antibodies is to be found by the appropriate pathogen in order to get rid of the pathogen.  There are a few different types of antibodies.  There are monovalent and bivalent antibodies in the body, a monovalent antibody is like the antibody grabbing on to the pathogen with one arm.  Whereas a bivalent antibody would be like grabbing on with two arms.  A bivalent antibody obviously would be a better choice because the bond is stronger because the the increased number of bonds formed.  Also, it depends on the valency of the antibody to determine how complex of a structure it will form. For example the more valent it is, the larger it can be, creating more bonds.  Once these antibodies are made there are several ways that a person can harvest them from the test sample.  The most common laboratory way is to use a centrifuge to separate and purify the complexes.  However, all this takes money in order to research to develop.

To give you a sense of the amount of binding strength that took place, he  plotted the mole fraction against the ligand concentration as it increased. He also found that trivalent binding yielded more complex structures. In his research, he wanted to form structures without steric hindrance and was excited that he found a ligand that could bind three arms of the antibody. At the end of his research, he was able to find that bivalent and trivalent ligands promote stable aggregates of antibodies and that antibodies are bivalent since this increases the time of attachment, increasing production, as I stated before.

Overall, I thought his presentation was pretty interesting. He spoke clearly and was able to deliver his message clearly without much confusion. He kept his information relatively easy to understand and follow so that students wouldn’t get too lost or disinterested.  I personally, would recommend Dr. Bilgicer to speak again in the future.

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Dr. Basar Bilgicer was the featured presenter at this week’s ChemSem installment. The simple focus of his presentation worked upon the well known chemical fact that two bonds are better than one. A complex organism produces antibodies which, upon encountering a foreign antigen, attach to its surface. When a large number of these antibodies attach, the mass and concentration triggers and immune response which works to expel the antigen from the system now that it has been identified. Often, the binding antibodies are monovalent having one site which bonds to the antigen. However, if antibodies are available that are divalent, they can bond to the antigen in more than one site, keeping them from detaching and encouraging the immune response.

Admittedly there were several portions of this presentation which were beyond my understanding of nature. I never focused much on either biology or biochemistry, and it took some catching up in order to grasp the material. I was curious to find out why the divalent antibodies didn’t slow immune response considering the fact that they bound twice as many antigen sites but only developed half the antibody density. Furthermore, it was unclear whether these antibodies were entirely synthetic (it appeared as if they were) and therefore had unknown internal biochemistry in organisms. Bilgicer did admit that the conditions of his trials on the divalent antibodies were significantly different than the internal circumstances to which they would ultimately be applied. Finally, I was interested to find that more than 35% of current pharmaceutical research was focused on antibody development, which seemed to suggest it was a much larger field than is publicized. Is the lack of notable material regarding it simply due to secrecy on the part of pharmaceutical corporations, or is the research still significantly in its infancy?

Regardless of all of this, the chemistry to precipitate and separate the antibodies from their respective solutions was explained in a straight-forward and clear manner and I thought overall Bilgicer did a good job of expressing his research and the efforts of his team in analyzing this material. In the end, though I didn’t fully understand the intricacies of the matter, the fundamental principles seem reasonable and well worth further study.

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Assistant chemical & biomolecular engineering professor from Notre Dame, Basar Bilgicer obviously was well qualified to do the presentation on amino acids and antibody, as he has worked on peptide design using unnatural amino acids while pursuing his PhD degree. His presentation was well-paced, ending right around the time when the seminar is supposed to be over, but over my head mostly, because I forgot a lot of things I learned in biology and biochemistry classes. However, the general idea of the presentation was easy to follow and understandable.

During his presentation, I learned that there are two kinds of antibodies (monovalent, which only binds on one spot, vs bivalent, which binds on two spots). To study bivalent antibodies, using two rigid seperate antigens or short antigen pairs so that the antigen pair cannot be binded by one antibody. In order for antibody and hapten (ligand) pair to occur, tight bonding and easily modified hapten structure are necessary. I was also reminded of size exclusion chromatography that allows the larger molecules to come out faster than the smaller ones using porous gels. I learned that antibody cyclic aggregates provides higher stability due to bivalency, and sufficient  concentration is necessary in forming antibody complexes. One good application of an antibody complex was pharmaceutical companies making drugs from it.

Three questions I came up with duing his presentations were 1) what is hapten? is it same as antigens ?, 2) would stability increase continuously as more antibody aggregates to form antibody complexes?, and 3) are the antibodies you used made commercially or by humans?

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For this seminars topic the presenter, Basar Bilgicer, allowed the audience to choose the topic that they would like to here him present on.  The topic of choice was Multivalent Antibody Aggregation.  However, before we get into his talk here is a little background on our presenter.  Basar Bilgicer was born in Istanbul and received his undergraduate degree in Chemistry at Bogaziki University in Turkey.  In 1999 he found himself in Boston pursuing his PhD in Chemistry at Tufts University, where he worked on peptide design using unnatural amino acids.  As a graduate student he published several first author articles and some of his work was even highlighted by Chemical and Engineering News.  After earning his PhD in 2004 Basar Biligicer moved to George Whitesides group in the Department of Chemistry and Chemical Biology at Harvard University.  Since then he has been working to understand the thermodynamics and kinetics of multivalent interactions, more specifically the association of bivalent antibodies.  Basar Bilgicer is currently working-on research at the University of Notre Dame where he concentrates on designing multivalent molecules for diagnostic and therapeutic applications for cancer, autoimmune diseases and allergies.

Now that we have a little background, here is what Basar Bilgicer had to say about Multivalent Antibody Aggregation. One of the major challenges for Antibodies is to be found by the appropriate pathogen in order to get rid of the pathogen.  There are a few different types of antibodies.  There are monovalent antibodies which is similar to having the antibody grab onto the pathogen with one arm.  Whereas bivalent antibodies would be similar to grabbing on with two arms.  A bivalent antibody obviously would be a better choice because the bond is stronger because the the increased number of bonds formed.  Also, it depends on the valency of the antibody to determine how complex of a structure it will form. For example the more valent it is the larger it can become creating more bonds.  Once these antibodies are made there are several ways that a person can harvest them from the test sample.  The most common laboratory way is to use a centrifuge to separate and purify the complexes.  However, all this takes money in order to research to develop.  The money tree has not been invented yet so until there is one research in this field for most individuals is very limited.

Even though Basar Bilgicer had a really cool and interesting topic he did not seem to portray that in his presentation.  I felt that his presentation was very dry and almost dull.  He seemed monotone for most of his talk so following and understanding him was a challenge.  He seemed to like his topic but he did not seem excited to share his topic.  He had vast knowledge of his topic so therefore he was excited about his stuff but sharing it seemed to lack emphasis and enthusiasm.  Overall he was extremely nice and even finished on time. Great job overall.

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The past week speaker, Basar Bilgicer, is a faculty member from Notre Dame University. He came to give a presentation on peptide design and multivalent antibodies. More specifically, he was examining the IgG antibody. He first explained to us the basics of antibodies and how they have binding sites for antigens. The Immunoglobulin G (IgG) antibody had two binding sites for antigens. The antibody itself looks similar to a “Y” in shape and is composed of light chains and heavy chains.

So the purpose of his research was to examine monovalent and bivalent antibodies. It was interesting to see how entropy was payed off between the monovalent and bivalent because the antibody arms were linked together. Bilgicer then did further investigation where he used substrates that were linked together close enough so that they wouldn’t bind to the same antibody in different arms. He then did some chromatography with a column of beads where different sizes resulted in different rates of falling through the column. Large would fall first, while smaller one got caught inside the holes in the beads and took longer to pass through the column. He found that there were bivalent and trivalent formations of the antibodies.

Overall, I thought his presentation was pretty interesting. He spoke clearly and was able to deliver his message clearly without much confusion. He kept his information relatively easy to understand and follow so that students wouldn’t get too lost or disinterested. He finished well below the allotted time allowed which provided for ample time for the Q&A period, which was utilized well.

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Originally from Istanbul and now at Notre Dame, Basar Bilgicer seems to have quite an impressive resume. Currently he is studying the characteristics of multivalent reactions, specifically bivalent antibodies. His voice has a notable accent but it did not affect communication. At first, his presentation style was teacher-like but after covering basic information (such as the shape of antibodies) and asking if the audience had taken a course in biochemistry, he went deeper into the material.

Multivalent reactions are favorable as the amount of entropy for multiple bonds costs the same amount of entropy for a single bond in the same conditions. So the amount of free energy increases for a bivalent bond relative to a monovalent bond. To study these reactions, Bilgicer used hapten, a ligand whose response is related to pain sensory. It binds to antibodies but does not cause an immune reaction. As well as studying the thermodynamic and kinetic aspects of multivalent reactions, Bilgicer and his team of researchers work on the design of various drugs. Multiple bonds result in stronger attachments, which mean longer attachments. The illustration Bilgicer used was using two arms to hold on to an object instead of one.

Bilgicer’s research illustrates how something very basic as the form of the antibody can yield improvements in medicine by understanding the function. While the level of understanding the concept of multivalent reactions was simple, the process in researching and proving and understanding the reactions at a deeper level proved to be trickier than I thought.

Laymen’s Summary of Chemistry Seminar: Your immune response involves antigens and antibodies. Your body has a wide variety of antibodies which match up to an equally impressive variety of antigens. Certain antigens mean that something foreign and likely unwanted has invaded your body and when they bind to antibodies, your immune response kicks in. Now antibodies are Y shaped and two of those ends are antigen-binding sites. Why two? Bilgicer says that this is because that makes a stronger, longer bonding session, which equals to better in most cases. Bilgicer’s research can help create medicinal answers to improve therapy.

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This week’s speaker was Basar Bilgicer, who presented on multivalent antibodies. This speaker had was low voiced which made his presentation somewhat tough to follow. Bilgicer is a Chemical and Biomolecular engineer and was once a Harvard graduate, currently employed at Notre Dame University. This presentation went by quickly, but there was time towards the end when, Biglicer was able to answer any questions. I found this topic to be very interesting and I was able to learn many new things about antibody binding and other characteristics.

I learned that antibodies have avidity to binding from bivalency. Antibodies can be either monovalent or bivalent, in which they either bind one arm or both. They have a “Y” shaped structure in which there are two heavy chains and two light chains joined to form this shape. When an antibody binds with both arms the bond tends to be tighter or stronger. Biglicer researched the making of a synthetic antibody structure and wanted to make sure that this structure was tight binding, had a hapten structure that could be easily modified, commercially available, and a good price for making an antibody ligand pair. I also learned that the relationship between the monovalent and bivalent binding when dealing with enthalpy is the same. This happens due to the fact that although they are bivalent in bonding the arms would end up coming down at the same time yielding the same values as the monovalent ligand.

To give them a sense of the amount of binding/ binding strength that took place, they would plot the mole fraction against the ligand concentration as it increased. They also found that trivalent binding yielded more complex structures. In their research they wanted to form structures without steric hindrance and were excited that they found a ligand that could bind three arms of the antibody. At the end of their research they were able to find that bivalent and trivalent ligands promote stable aggregates of antibodies and that antibodies are bivalent since this increases the time of attachment, increasing production.

Many students seemed to enjoy the presentation and were very interested in learning more about antibodies. It’s interesting that pharmaceutical companies are trying to create more efficient antibodies than the ones in our bodies. There were many questions toward the end and Biglicer was able to answer them well. The presentation did encourage me to learn more about this topic, but not enough to do graduate research on it. Biglicer didn’t really tell much about attending his school of graduate studies, but he was available to answer questions about it. This presentation told of the binding properties of antibodies and their characteristics.

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Dr. Basar Bilgicer came from Notre Dame and talked with us about “Multivalent Antibody Aggregation”. He started out by asking which subject we would like to learn about, since he originally was going to rush through two different subject matters. We chose the one on antibodies, and he went with it.

He talked about the difference between a monovalent antibody vs a bivalent antibody and the significance of bivalent bonding. One interesting technique that he talked about was the non-chromatographic purification method. The solution is centrifuged to cause all the larger and heavier proteins to collect at the bottom of the test tube. The pellet is removed, and the remaining solution is mixed with excess antigens. The new solution is again centrifuged, and since excess antigens were added the antibodies binded to them and created heavier molecules. After the second centrifugation these heavier molecules collected in the bottom of the test tube, and then were removed. They were resuspended and treated so the antibodies were again singular.

The seminar as a whole was nice, the material being very interesting. Dr. Bilgicer voice was a little quiet and not very engaging, but he did a good job. If I was going to describe this seminar to a non-scientific person I would say that it was about the clustering of antibodies, and making them respond in desired fashions.

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Today’s speaker was Basar Bilgicer from the University of Notre Dame.  His study was focused on the antibodies to the protein IgG.  First, he explained the basics of antibodies.  Antibodies consist of light and heavy chains that are attracted to each other by disulfide bonds.  Antibodies have multiple limbs, or ligands.  If two ligands are used for binding, that antibody is bivalent.  If someone holds onto an object with two hands, that will be a stronger grip than using just one hand.  It is the same way with antibodies.  However, while this increases the enthalpy, it also decreases the entropy, making the binding less favorable.  The distance between the ligands on the antibodies varies, so it is impossible to specifically position a ligand onto a surface.  One approach is to synthesize a linker that is soluble in water, but that is usually very difficult.  Instead, very short linkers are made, one binding to each ligand.  One major challenge is that antibodies are very expensive to purchase (the cheapest antibody is $350 for 50 micrograms).  Also, tight binding needs to occur between antibodies and antigens, and the structures must be easily modified.

The behavior of antibodies and antigens is quite complex.  Sometimes, the antigens will bind directly to the ligands.  Other times, cyclizations will occur, forming dimers and trimers of antibodies.  These cyclic aggregates are very stable due to bivalency and trivalency.  The concentrations of the antibodies and antigens affects the type of complex formed.  The practical application to this research is that drugs could be designed using these stable aggregates.

I found this presentation to be interesting because of the potential applications.  The speaker moved quite rapidly, so it was difficult to understand at times.  That being said, I highly respect the speaker for not going over the alloted seminar time.  I wanted to know how many different antibodies had been studied by Bilgicer.  He reminded me that the high price of antibodies limits what he can research, so the answer was not very many.  I am also interested to know how many multivalent antibodies exist compared to monovalent antibodies.  I am sure that if multivalency is necessary for stability, the ratio should be quite high.  Finally, I want to know why the protein IgG was specifically chosen for this study.  What is special about this particular protein?  If I had to sum up this presentation for a layperson, I would say that the stability of antibodies with multiple arms was investigated.

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The seminar this week was presented by Dr. Basar Bilgicer. Dr. Bilgicer is from the Department of Chemical and Biochemical Engineering at the University of Notre Dame. I cannot say that I enjoyed the topic of discussion as well as I have other seminar topics. I did not find it very interesting, mainly because it very much reminded me of the cellular molecular biology class I took last year while attending Penn State. I became lost after several slides of presentation and could not seem to catch up with what the speaker was talking about.

One thing that I learned from this lecture is that trivalent ligands yield more complex structures and promote a bicyclic antibody trimer. Another thing that I learned was that around fifty-five percent of pharmaceutical research being done today is focused on synthetic antibody production. This is in part because of a discovery that antibody treatment is an excellent way to fight off disease because of the natural use of antibodies by the body to fight off disease and the relatively low side effects that the treatment produces.

From my limited grasp of what the speaker was talking about, if describing what this seminar was about to a non-science friend, I would have to say that it was about how antibodies work to fight disease and how we can use them for future medical techniques. As for the speaker, he seemed genuinly interested in his topic of research, but he was a little too quiet in his presentation and sometimes slightly hard to understand. Of course, it would probably have helped if I had gotten a little more sleep the night before.

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The day before this seminar I was tutoring a student in Biology about T cells, B cells, antigens and antibodies. I was pleasantly surprised to have a presentation entitled Multivalent Antibody Aggregation last Thursday. The presentation was given by Basar Bilgicer from Notre Dame University.

The presentation focused around the question of how tightly bivalent antibodies bind. A bivalent bonding of antibodies means that both “arms” of the molecule are bound to a ligand. This is opposed to a monovalent binding in which only one arm of the antibody is bound to the ligand. The “head” of an antibody can bind to another and create a dimer. Antibodies specifically need tight bonding and a hapten structure that is easily modified. Hapten structure is one that binds to an antibody with no response.

Two of the techniques described for this experimental research were size exclusion chromatography and centrifugation. Size exclusion chromatography is somewhat backwards to the common idea of chromatography. Normally the smallest molecules exit the column first and large molecules take more time to filter their way out. Size exclusion chromatography uses beads that trap the small molecules so only the large molecules, to bit to fit into the bead crevasses, come out of the column.  Multiple centrifuge techniques move the proteins to the outer wall of the tube so purification can take place.

The practical use of this research pertains to pharmaceutical work. Antibodies are produced outside the body and injected into the body with very few side effects. This research will help design better drugs with reduced toxic effects.

In describing this seminar to a friend or family member I would say we learned about antibodies and how they bind to fight infection.

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This week’s chemistry seminar was presented by Dr. Basar Bilgicer. Dr. Bilgicer is an assistant professor of the Department of Chemistry and Biochemistry at University of Notre Dame. The topic Dr. Bilgicer presented was on multivalent antibodies. Dr. Bilgicer spoke with a clear tone that was easy to understand. However he did have an accent that sometimes made it harder to understand him.

According to him, multivalent interactions between molecules are crucial in our biological systems. By understanding the thermodynamics and kinetics of these interactions, the development of new ways to treat diseases and diagnose them can be found. His research more specifically focused on how multivalent antibodies form complexes of these antibodies.

Some new information I learned from this week’s seminar includes the fact that different antibody complexes can be formed. I always thought that antibodies just formed a clump when bound to the antigen. To see that there was a specific order and conformation to this binding was very interesting. Also the fact that antibodies were expensive was a surprise, since I had always thought that antibodies were very common and numerous because of how many an organism’s body makes. Another new piece of information I found out from the presentation was that there is a specific distance between the two binding sites of the antibody that also determines the conformation. I had always thought that antibodies were exactly the same, except for the binding sites, which determined what antigen it was bound to.

Overall, his topic was very interesting, and was very well presented. Although I had a little trouble understanding him because of unfamiliarity of some terms, this topic definitely sparked my interest.

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