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.
By:
Kuan Hu Imprint: Springer Verlag, Singapore Country of Publication: Singapore Edition: 2021 ed. Dimensions:
Height: 235mm,
Width: 155mm,
Weight: 197g ISBN:9789813366152 ISBN 10: 981336615X Series:Springer Theses Pages: 102 Publication Date:27 January 2022 Audience:
Professional and scholarly
,
Undergraduate
Format:Paperback Publisher's Status: Active
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.