Hidden Bibliographic Details
| ISBN: | 9789813366138
9813366133
9813366125
9789813366121
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| Notes: | "Doctoral thesis accepted by Peking University, Beijing, China."
Includes bibliographical references.
Online resource; title from PDF title page (SpringerLink, viewed March 9, 2021).
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| Summary: | 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. .
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| Other form: | Print version: 9789813366121
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| Standard no.: | 10.1007/978-981-33-6613-8
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