Structure-activity study of macropin, a novel antimicrobial peptide from the venom of solitary bee Macropis fulvipes ( Hymenoptera: Melittidae)

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10218709" target="_blank" >RIV/00216208:11310/14:10218709 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/14:00429456

Result on the web

<a href="http://dx.doi.org/10.1002/psc.2625" target="_blank" >http://dx.doi.org/10.1002/psc.2625</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/psc.2625" target="_blank" >10.1002/psc.2625</a>

Result language

angličtina

Original language name

Structure-activity study of macropin, a novel antimicrobial peptide from the venom of solitary bee Macropis fulvipes ( Hymenoptera: Melittidae)

Original language description

A novel antimicrobial peptide, designated macropin (MAC-1) with sequence Gly-Phe-Gly-Met-Ala-Leu-Lys-Leu-Leu-Lys-Lys-Val-Leu-NH2, was isolated from the venom of the solitary bee Macropis fulvipes. MAC-1 exhibited antimicrobial activity against both Gram-positive and Gram-negative bacteria, antifungal activity, and moderate hemolytic activity against human red blood cells. A series of macropin analogs were prepared to further evaluate the effect of structural alterations on antimicrobial and hemolytic activities and stability in human serum. The antimicrobial activities of several analogs against pathogenic Pseudomonas aeruginosa were significantly increased while their toxicity against human red blood cells was decreased. The activity enhancement is related to the introduction of either l- or d-lysine in selected positions. Furthermore, all-d analog and analogs with d-amino acid residues introduced at the N-terminal part of the peptide chain exhibited better serum stability than did na

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

<a href="/en/project/GA203%2F08%2F0536" target="_blank" >GA203/08/0536: Antimicrobial peptides from insects for possible therapeutic applications</a><br>

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

6

Country of publishing house

GB - UNITED KINGDOM

Number of pages

10

Pages from-to

375-384

UT code for WoS article

000335549200001

EID of the result in the Scopus database

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