报告题目：Structure-Based Design, Synthesis and Applications of a New Class of Peptidomimetics: γ-AA Peptides and Their Derivatives

报 告 人：苏玛（南佛罗里达大学）

报告时间：2019年5月7日（星期二）15:00

报告地点：药学院云轩楼1323会议室

报告人简介：

Ma Su held her PhD in Chemistry from University of South Florida in December 2018. Her ph.D work focuses on the development of antimicrobial agents and development of peptidomimetics-based combinatorial library for the identification of potential drug candidates and leads. She developed a series of drug-like molecules which display broad-spectrum activity against both Gram-positive and Gram-negative multidrug-resistant bacterial pathogens. The results have been published J. Med. Chem. She also developed polymyxin derivatives which show excellent activity against bacteria. In addition, she discovered a new class of lipidated small molecules which largely suppress the bacteria growth.

报告摘要：

Peptidomimetics can mimic hierarchical structures of peptides and proteins. Thus, they are extensively studied for therapeutic applications. To break the limitation of backbones and frameworks and expand the peptidomimetics family, a new class of peptidomimetics - “γ-AApeptides” was developed. Design of γ-AApeptides is based on the chiral peptide nucleic acids (PNAs) backbone.

The World Health Organization estimates that one third of all deaths in the world are on account of infectious diseases. AMPs are important because of their high activity against broad spectrum microbes, less susceptible to grow resistance and selectivity in binding to bacterial cells over human cells. γ-AApeptides as a new class of peptidomimetics have increased stability and enhanced chemical diversity. We have developed polymyxin mimic cyclic peptides, small linear molecules and hydantoin derivatives as potent antibiotic agents with γ-AApeptides. They have good bioactivity and selectivity.

Combinatorial library is key technology for accelerating the discovery of novel therapeutic agents. One-bead-two-compound γ-AApeptides-based library was developed and screened against SMYD2 protein which is essential for tumor growing.