Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00384565" target="_blank" >RIV/61388963:_____/12:00384565 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s00726-012-1283-1" target="_blank" >http://dx.doi.org/10.1007/s00726-012-1283-1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00726-012-1283-1" target="_blank" >10.1007/s00726-012-1283-1</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera

Popis výsledku v původním jazyce

Introducing all-hydrocarbon staples into short alpha-helical amphipathic antimicrobial peptides increases their hydrophobicity, hydrophobic moment, rigidity and generally alpha-helicity in water. Stapling generally makes the peptides more resistant to proteolytic degradation, particularly those that are doubly stapled. The introduction of olefinic amino acid residues and conformational restriction by stapling make the peptides significantly more hemolytic, and lead to a decrease of their antimicrobial potency against pathogenic bacteria. Unfortunately, the stapling of those peptides is not rendering compounds that would have better pharmacological qualities than the native unmodified potent peptides.

Název v anglickém jazyce

Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera

Popis výsledku anglicky

Introducing all-hydrocarbon staples into short alpha-helical amphipathic antimicrobial peptides increases their hydrophobicity, hydrophobic moment, rigidity and generally alpha-helicity in water. Stapling generally makes the peptides more resistant to proteolytic degradation, particularly those that are doubly stapled. The introduction of olefinic amino acid residues and conformational restriction by stapling make the peptides significantly more hemolytic, and lead to a decrease of their antimicrobial potency against pathogenic bacteria. Unfortunately, the stapling of those peptides is not rendering compounds that would have better pharmacological qualities than the native unmodified potent peptides.

Druh

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

CEP obor

CC - Organická chemie

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

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Amino Acids

ISSN

0939-4451

e-ISSN

—

Svazek periodika

43

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

AT - Rakouská republika

Počet stran výsledku

12

Strana od-do

2047-2058

Kód UT WoS článku

000309863400022

EID výsledku v databázi Scopus

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