Synthesis of lucifensin by native chemical ligation and characteristics of its isomer having different disulfide bridge pattern

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00431796" target="_blank" >RIV/61388963:_____/14:00431796 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1002/psc.2663" target="_blank" >http://dx.doi.org/10.1002/psc.2663</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/psc.2663" target="_blank" >10.1002/psc.2663</a>

Result language

angličtina

Original language name

Synthesis of lucifensin by native chemical ligation and characteristics of its isomer having different disulfide bridge pattern

Original language description

The antimicrobial 40-amino-acid-peptide lucifensin was synthesized by native chemical ligation (NCL) using N-acylbenzimidazolinone (Nbz) as a linker group. NCL is a method in which a peptide bond between two discreet peptide chains is created. Thismethodhas been applied to the synthesis of long peptides and proteins when solid-phase synthesis is imcompatible. Two models of ligation were developed: [15 + 25] Ala-Cys and [19 + 21] His-Cys. The [19 + 21] His-Cys method gives lower yield because of the lower stability of 18-peptide-His-Nbz-CONH2 peptide, as suggested by density functional theory calculation. Acetamidomethyldeprotection and subsequent oxidation of the ligated linear lucifensin gave a mixture of lucifensin isomers, which differed in the location of their disulfide bridges only. The dominant isomer showed unnatural pairing of cysteines [C1 - 6], [C3 - 5], and [C2 - 4], which limits its ability to form alpha-helical structure. The activity of isomeric lucifensin toward Bacill

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Peptide Science

ISSN

1075-2617

e-ISSN

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Volume of the periodical

20

Issue of the periodical within the volume

9

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

725-735

UT code for WoS article

000340423800008

EID of the result in the Scopus database

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