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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388963:_____/14:00429456

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F08%2F0536" target="_blank" >GA203/08/0536: Antimikrobiální peptidy z hmyzu pro možná terapeutická využití</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Peptide Science

ISSN

1075-2617

e-ISSN

—

Svazek periodika

20

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

375-384

Kód UT WoS článku

000335549200001

EID výsledku v databázi Scopus

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