Development of In-Tether Carbon Chiral Center-Induced Helical Peptide [electronic resource] : Methodology and Applications / by Kuan Hu.
- Hu, Kuan
- Singapore : Springer Singapore : Imprint: Springer, 2021.
- 1st ed. 2021.
- Physical Description:
- XV, 102 pages 75 illustrations, 65 illustrations in color : online resource
- Additional Creators:
- SpringerLink (Online service)
- Springer Theses, Recognizing Outstanding Ph.D. Research, 2190-5053
- 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.
- 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. .
- Digital File Characteristics:
- PDF and text file
View MARC record | catkey: 32863588