The use of Fmoc-Lys(Pac)-OH and penicillin G acylase in the preparation of novel semisynthetic insulin analogs

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F07%3A00081724" target="_blank" >RIV/61388963:_____/07:00081724 - 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

The use of Fmoc-Lys(Pac)-OH and penicillin G acylase in the preparation of novel semisynthetic insulin analogs

Original language description

We present the synthetic protocol and characterization of Fmoc-Lys(Pac)-OH, its use for the preparation of octapeptides H-Gly-Phe-Tyr-N-MePhe-Thr-Lys(Pac)-Pro-Thr-OH and H-Gly-Phe-Phe-His-Thr-Pro-Lys(Pac)-Thr-OH by solid-phase synthesis, trypsin-catalyzed condensation of these octapeptides with desoctapeptide(B23-B30)-insulin, and penicillin G acylase catalyzed cleavage of phenylacetyl (Pac) group from N-amino group of lysine to give novel insulin analogs [TyrB25, N-MePheB26,LysB28,ProB29]-insulin and [HisB26]-insulin.

Czech name

Užití Fmoc-Lys(Pac)-OH a penicilin G acylázy při přípravě nových semisyntetických analogů insulinu

Czech description

Článek prezentuje detailní syntézu a charakterizaci Fmoc-Lys(Pac)-OH a jeho užití při syntéze dvou oktapeptidů syntézou peptidů na pevné fázi, trypsinem katalyzovanou semisyntézu oktapeptidů s desoktapeptid(B23-B30)-insulinem a štěpení fenylacetylové skupiny penicilin G acylázou z epsilon-aminoskupiny lysinu.

Type

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

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/LC06077" target="_blank" >LC06077: Center of Chemical Genetics</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2007

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

13

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

334-341

UT code for WoS article

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EID of the result in the Scopus database

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