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Development of In-Tether Carbon Chiral Center-Induced Helical Peptide

Methodology and Applications

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  • © 2021

Overview

  • Nominated as an outstanding PhD thesis by Peking University
  • Reports on important progress in the study of stabilized peptide drugs
  • Introduces applications in cancer stem cell therapy and self-assembly for novel nanomaterials
  • Includes a diversity-oriented synthesis methodology for constructing stabilized peptides and a clear study of the correlation between peptides’ structure and their biophysical/biochemical properties

Part of the book series: Springer Theses (Springer Theses)

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Table of contents (4 chapters)

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About this book

This book focuses on the development of stapled peptides, a novel molecular modality used to regulate aberrant intracellular protein–protein interactions (PPIs). The author designs and presents a novel helical peptide stabilization methodology by constructing a chiral cross-linker moiety, namely “chiral center induced peptide helicity (CIH)”. The book demonstrates that a precisely positioned carbon chiral center on tether can decisively determine the secondary structure of a peptide, and that the R-configured peptide is helical, while the S-configured peptide is non-helical. Further, it reports that helicity-enhanced R isomer peptides displayed significantly enhanced cell permeability and target binding affinity, as well as tumor inhibition efficiency, in comparison to S isomer peptides. The book will not only advance readers’ understanding of the basic principle of stapled peptides, but also accelerate the clinical transformation of stapled peptide drugs. 

Authors and Affiliations

  • School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China

    Kuan Hu

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