國立虎尾科技大學 |

Development of In-Tether Carbon Chiral Center-Induced Helical Peptide = Methodology and Applications /

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Development of In-Tether Carbon Chiral Center-Induced Helical Peptide/ by Kuan Hu.
Reminder of title:	Methodology and Applications /
Author:	Hu, Kuan.
Description:	XV, 102 p. 75 illus., 65 illus. in color.online resource. :
Contained By:	Springer Nature eBook
Subject:	Bioorganic chemistry. -
Online resource:	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. - 1st ed. 2021. - XV, 102 p. 75 illus., 65 illus. in color.online resource. - Springer Theses, Recognizing Outstanding Ph.D. Research,2190-5061. - Springer Theses, Recognizing Outstanding Ph.D. Research,.

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:

743635
Bioorganic chemistry.

LC Class. No.: QD241-441

Dewey Class. No.: 547

Development of In-Tether Carbon Chiral Center-Induced Helical Peptide = Methodology and Applications /
LDR:02705nam a22004095i 4500 001 1052400
003 DE-He213
005 20210819081031.0
007 cr nn 008mamaa
008 220103s2021 si | s |||| 0|eng d
020 $a 9789813366138 $9 978-981-33-6613-8
024 7 $a 10.1007/978-981-33-6613-8 $2 doi
035 $a 978-981-33-6613-8
050 4 $a QD241-441
072 7 $a PSB $2 bicssc
072 7 $a SCI013040 $2 bisacsh
072 7 $a PSB $2 thema
082 0 4 $a 547 $2 23
100 1 $a Hu, Kuan. $e author. $4 aut $4 http://id.loc.gov/vocabulary/relators/aut $3 1357115
245 1 0 $a Development of In-Tether Carbon Chiral Center-Induced Helical Peptide $h [electronic resource] : $b Methodology and Applications / $c by Kuan Hu.
250 $a 1st ed. 2021.
264 1 $a Singapore : $b Springer Singapore : $b Imprint: Springer, $c 2021.
300 $a XV, 102 p. 75 illus., 65 illus. in color. $b online resource.
336 $a text $b txt $2 rdacontent
337 $a computer $b c $2 rdamedia
338 $a online resource $b cr $2 rdacarrier
347 $a text file $b PDF $2 rda
490 1 $a Springer Theses, Recognizing Outstanding Ph.D. Research, $x 2190-5061
505 0 $a 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.
520 $a 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. .
650 0 $a Bioorganic chemistry. $3 743635
650 0 $a Proteins . $3 1253493
650 0 $a Biomaterials. $3 677000
650 0 $a Biochemical engineering. $3 654817
650 0 $a Cancer research. $3 1253664
650 1 4 $a Bioorganic Chemistry. $3 677511
650 2 4 $a Protein-Ligand Interactions. $3 882815
650 2 4 $a Biochemical Engineering. $3 593907
650 2 4 $a Cancer Research. $3 668358
710 2 $a SpringerLink (Online service) $3 593884
773 0 $t Springer Nature eBook
776 0 8 $i Printed edition: $z 9789813366121
776 0 8 $i Printed edition: $z 9789813366145
776 0 8 $i Printed edition: $z 9789813366152
830 0 $a Springer Theses, Recognizing Outstanding Ph.D. Research, $x 2190-5053 $3 1253569
856 4 0 $u https://doi.org/10.1007/978-981-33-6613-8
912 $a ZDB-2-CMS
912 $a ZDB-2-SXC
950 $a Chemistry and Materials Science (SpringerNature-11644)
950 $a Chemistry and Material Science (R0) (SpringerNature-43709)