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Development of in-tether carbon chir...

Hu, Kuan.

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Development of in-tether carbon chiral center-induced helical peptide = methodology and applications /

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Development of in-tether carbon chiral center-induced helical peptide/ by Kuan Hu.
其他題名:	methodology and applications /
作者:	Hu, Kuan.
出版者:	Singapore :Springer Singapore : : 2021.,
面頁冊數:	xv, 102 p. :ill. (some col.), digital ;24 cm.
內容註:	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.
Contained By:	Springer Nature eBook
標題:	Peptides - Biotechnology. -
電子資源:	https://doi.org/10.1007/978-981-33-6613-8
ISBN:	9789813366138

Development of in-tether carbon chiral center-induced helical peptide = methodology and applications /
Hu, Kuan.

Development of in-tether carbon chiral center-induced helical peptidemethodology 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

Standard No.: 10.1007/978-981-33-6613-8doiSubjects--Topical Terms:

916554
Peptides
--Biotechnology.

LC Class. No.: QP552.P4 / H858 2021

Dewey Class. No.: 572.65

Development of in-tether carbon chiral center-induced helical peptide = methodology and applications /
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