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Development of in-tether carbon chir...
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Hu, Kuan.
Development of in-tether carbon chiral center-induced helical peptidemethodology and applications /
Record Type:
Electronic resources : Monograph/item
Title/Author:
Development of in-tether carbon chiral center-induced helical peptideby Kuan Hu.
Reminder of title:
methodology and applications /
Author:
Hu, Kuan.
Published:
Singapore :Springer Singapore :2021.
Description:
xv, 102 p. :ill. (some col.), digital ;24 cm.
Contained By:
Springer Nature eBook
Subject:
PeptidesBiotechnology.
Online resource:
https://doi.org/10.1007/978-981-33-6613-8
ISBN:
9789813366138$q(electronic bk.)
Development of in-tether carbon chiral center-induced helical peptidemethodology and applications /
Hu, Kuan.
Development of in-tether carbon chiral center-induced helical peptide
methodology and applications /[electronic resource] :by Kuan Hu. - Singapore :Springer Singapore :2021. - xv, 102 p. :ill. (some col.), digital ;24 cm. - Springer theses,2190-5053. - Springer theses..
Introduction -- Method to construct in-tether chiral center constrained helical peptide -- Application in disrupting p53/MDM2 protein-protein interactions -- Fabrication of nanomaterials with in-tether chiral center constrained helical peptide.
This book focuses on the development of stapled peptides, a novel molecular modality used to regulate aberrant intracellular protein-protein interactions (PPIs) The author designs and presents a novel helical peptide stabilization methodology by constructing a chiral cross-linker moiety, namely "chiral center induced peptide helicity (CIH)". The book demonstrates that a precisely positioned carbon chiral center on tether can decisively determine the secondary structure of a peptide, and that the R-configured peptide is helical, while the S-configured peptide is non-helical. Further, it reports that helicity-enhanced R isomer peptides displayed significantly enhanced cell permeability and target binding affinity, as well as tumor inhibition efficiency, in comparison to S isomer peptides. The book will not only advance readers' understanding of the basic principle of stapled peptides, but also accelerate the clinical transformation of stapled peptide drugs.
ISBN: 9789813366138$q(electronic bk.)
Standard No.: 10.1007/978-981-33-6613-8doiSubjects--Topical Terms:
220382
Peptides
--Biotechnology.
LC Class. No.: QP552.P4 / H858 2021
Dewey Class. No.: 572.65
Development of in-tether carbon chiral center-induced helical peptidemethodology and applications /
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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.
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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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Chemistry and Materials Science (SpringerNature-11644)
based on 0 review(s)
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1圖書
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EB QP552.P4 H874 2021 2021
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1 records • Pages 1 •
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https://doi.org/10.1007/978-981-33-6613-8
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