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.
| Autorius: | Kuan Hu |
| Serija: | Springer Theses |
| Leidėjas: | Springer Nature Singapore |
| Išleidimo metai: | 2022 |
| Knygos puslapių skaičius: | 120 |
| ISBN-10: | 981336615X |
| ISBN-13: | 9789813366152 |
| Formatas: | 235 x 155 x 7 mm. Knyga minkštu viršeliu |
| Kalba: | Anglų |
Parašykite atsiliepimą apie „Development of In-Tether Carbon Chiral Center-Induced Helical Peptide: Methodology and Applications“
