Biochemistry & Metabolomics

Biography:

Abstract:

Biography:

Dr. Vaughn Smider received his M.D. and Ph.D. degrees from Stanford University School of Medicine.  He is currently on the faculty of the Scripps Research Institute in the Cell and Molecular Biology Department, and is also the Chief Scientific Officer of Sevion Therapeutics.  Dr. Smider’s research focuses on both basic biology and applied technology in the antibody field, including antibody genetics, structure, engineering and development.

Abstract:

Typical mouse or human antibodies have CDR H3 loop lengths of 10-15 amino acids, which often form a flat binding surface for contact with antigen.  In contrast, cows can form CDR H3 regions of over 70 amino acids, which form novel ‘stalk’ and ‘knob’ domains that protrude far from the antibody surface.  These antibodies utilize an unusual diversity generating system that alters cysteine positions and disulfide bonding patterns in the knob.  The functional importance of this antibody system is illustrated by recent experiments showing that cows, unlike other species, can make a broad and potent neutralizing antibody response to spike antigens of HIV.

Biography:

Abstract:

Biography:

Orkid Coskuner-Weber is an expert in Alzheimer´s and Parkinso´s disease mechanism studies and monoclonal antibody design. She recived her Ph.D. degree from the Universitaet zu Koeln in Germany. She was a postdoc at Johns Hopkins and Stanford Universities. She was an assistant professor at George Mason University and at the University of Texas at San Antonio. She recently took a position in Istanbul for opening the Alzheimer´s and Parkinson´s disease research center. She has been associated with the National Institute of Standards and Technology since 2005. She develops and uses quantum chemical, statistical mechanical, bioinformatics, artificial intelligence and experimental tools in her research activities.

Abstract:

Alzheimer`s disease affects 10 million Americans and 44 million people worldwide. There are various biochemical mechanisms and processes that play a role in Alzheimer´s disease. These mechanisms are debated in the literature and there is currently no efficient drug that halts the progress of the disease. Efficient and effective drug design studies require detailed understanding of associated biochemical and biophysical mechanisms at the atomic level with dynamics. We investigate all biochemical processes and mechanisms associated with Alzheimer´s disease using quantum chemistry, statistical mechanics, bioinformatics, artificial intelligence and experiments. Using the information that we gain from biochemical investigations, we design monoclonal antibodies in collaboration with pharmaceutical companies. In this talk, we will present some of our studies about the roles of genetics, mitochondrial dysfunction and oxidative stress mechanisms in Alzheimer´s disease. Our theoretical and experimental results show that ATP reduces the fibrillization of disordered amyloid-β, transition metal ion coordination with amyloid-β increases the fibrillization progress and genetic factors significantly impact the fibrillization and aggregation properties of amyloid-β alloforms. Furthermore, we will provide insights into monoclonal antibody design for the treatment of Alzheimer´s disease.

Biography:

Jun-ichi Kadokawa received his Ph.D. in 1992. He then joined Yamagata University as a Research Associate. From 1996 to 1997, he worked as a visiting scientist at the Max-Planck-Institute for Polymer Research in Germany. In 1999, he became an Associate Professor at Yamagata University and moved to Tohoku University in 2002. He was appointed as a Professor of Kagoshima University in 2004. His research interests focus on polysaccharide materials. He received the Award for Encouragement of Research in Polymer Science (1997) and the Cellulose Society of Japan Award (2009). He has published more than 200 papers in academic journals.

Abstract:

Biological macromolecules, such as polysaccharide and protein (peptide) exhibit specific in vivo functions in living systems, which are appeared by their controlled primary and higher-order assembled structures. Many kinds of conjugates, which are assembled from such biological macromolecules, are present as vital materials in nature.  Therefore, artificial assemblies from biological macromolecules can be expected as new bio-based functional materials, which have a potential for practical applications in biomedical and tissue engineering fields. Polysaccharides are known to form nanostructured higher-order assemblies by non-covalent linkages such as hydrogen bonds. Accordingly, the construction of hierarchically assembled structures, so-called supramolecules, from polysaccharides has attracted much attention to obtain new polysaccharide-based functional materials. For example, amylose, which is a linear polysaccharide linked through a(1g4)-glycosidic linkages and well-known as a component of starch, forms regularly controlled assemblies, that is, inclusion complex and double helix, depending on whether guest compounds are present or not. Amylose with well-defined structure is synthesized by phosphorylase-catalyzed enzymatic polymerization using a-d-glucose 1-phosphate (G-1-P) and a(1g4)-oligoglucan (maltooligosaccharide) as monomer and primer, respectively. As the polymerization is initiated from the non-reducing end of the maltooligosaccharide primer, the enzymatic polymerization can be conducted using primers covalently linked to other polymeric materials (immobilized primers) at the reducing end, giving rise to amylose-grafted bio-based polymeric materials.^1,2 By means of the property of spontaneously double helix formation from the enzymatically synthesized amylose, the phosphorylase-catalyzed enzymatic polymerization using the immobilized primers produces supramolecular assemblies comprising the double helix cross-linking points.^3,4 For example, the phosphorylase-catalyzed enzymatic polymerization using the immobilized primers on chitin nanofibers was investigated to produce amylose-grafted chitin nanofiber assemblies.⁵ Owing to supramolecular network structure by the double helix cross-linking points, the product formed hydrogels, which were further converted into porous materials with controlled nano- and microstructures by lyophilization.