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

Methodology and Applications
1. Auflage 2021
ISBN: 978-981-336-613-8
Verlag: Springer Singapore
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 102 Seiten, eBook

Reihe: Springer Theses

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.

Zielgruppe

Research

Autoren/Hrsg.

Hu, Kuan

Inhaltsverzeichnis

Introduction.- Method to construct in-tether chiral center constrained helical peptide.- Application in disrupting p53/MDM2 protein-protein interactions.- Fabrication of nanomaterials with in-tether chiral center constrained helical peptide.