Analogues of AVP modified in the N-terminal part of the molecule with Pip isomers: TFA-catalysed peptide bond hydrolysis

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F09%3A00327400" target="_blank" >RIV/61388963:_____/09:00327400 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Analogues of AVP modified in the N-terminal part of the molecule with Pip isomers: TFA-catalysed peptide bond hydrolysis

Original language description

Synthesis and biological activity of 6 new AVP, [Mpa(1)] AVP and [Mpa(1),Val(4),D-Arg(8)]VP analogues modified in position 3 with L- or D-Pip, a non-coded alpha-imino acid, also called homoproline.

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

CC - Organic chemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2009

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

15

Issue of the periodical within the volume

3

Country of publishing house

GB - UNITED KINGDOM

Number of pages

5

Pages from-to

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UT code for WoS article

000263728100007

EID of the result in the Scopus database

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