Chemitope Glycopeptide is a Brooklyn-based biotechnology company specializing in the chemical synthesis of glycopeptides for research and clinical development. Leveraging two unique skill sets in carbohydrate and peptide chemistry, we exert atomic-level structural control to produce homogeneous complex glycopeptides. Chemitope’s research and development is focused on exploiting glycosylation in cancer and infectious diseases to develop glycopeptide immunogens for therapeutic and preventative vaccine applications. In addition, we provide comprehensive chemical synthesis and pre-clinical manufacturing support for our partners in academia, biotech, and the pharmaceutical industry.
Dr Baptiste Aussedat is an expert in the field of peptide and glycopeptide chemistry with over 18 years of experience. The results of his research have dramatically improved the efficiency of N-linked glycopeptide synthesis, which is foundational to the work of Chemitope Glycopeptide. Prior to co-founding Chemitope, Baptiste was a member of the Danishefsky lab at Memorial Sloan Kettering Cancer Center where he led a team that designed and synthesized glycopeptide immunogens for the Duke CHAVI-ID consortium and the NIH Vaccine Research Center. While in the Danishefsky lab, he also completed the first synthesis of a purely synthetic complex glycoprotein: the human Follicle-Stimulating Hormone (hFSH). Baptiste received his PhD in 2007 from the Pierre and Marie Curie University (now Sorbonne University) where he worked in the Laboratory of Biomolecules, under the direction of Dr. Gerard Chassaing, on the synthesis and biological evaluation of pseudo-peptides as intracellular drug delivery systems.
Dr William Walkowicz is an expert in complex glycan synthesis. His reliable methods have been leveraged to access dozens of glycan products necessary for the synthesis of complex N- and O-linked glycopeptides. Before co-founding Chemitope, Bill led efforts in the Danishefsky lab at Memorial Sloan Kettering Cancer Center to develop a scalable synthesis of high-mannose glycans for the synthesis of HIV glycopeptide immunogens. Bill received his PhD from the Gerstner Sloan Kettering Graduate School of Biomedical Sciences in the laboratory of David Y. Gin, where he made seminal contributions to the understanding of the structural basis of saponin immunoadjuvant activity.
Publications from the Chemitope Team
Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell (2021).
Cooperation between somatic mutation and germline-encoded residues enables antibody recognition of HIV-1 envelope glycans. PLoS Pathogens (2019).
Star nanoparticles delivering HIV-1 peptide minimal immunogens elicit near-native envelope antibody responses in nonhuman primates. PLoS Biology (2019).
HIV envelope V3 region mimic embodies key features of a broadly neutralizing antibody lineage epitope. Nature Communications (2018).
Staged induction of HIV-1 glycan–dependent broadly neutralizing antibodies. Science Translational Medicine (2017).
Mimicry of an HIV broadly neutralizing antibody epitope with a synthetic glycopeptide. Science Translational Medicine (2017).
Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman Primates. Cell Reports (2017).
Recognition of synthetic glycopeptides by HIV-1 broadly neutralizing antibodies and their unmutated ancestors. Proceedings of the National Academy of Sciences (2013).
Chemical Synthesis of Highly Congested gp120 V1V2 N-Glycopeptide Antigens for Potential HIV-1-Directed Vaccines. Journal of the American Chemical Society (2013).