Recombinant production of human antimicrobial peptide LL-37 and its secondary structure
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F23%3A00079276" target="_blank" >RIV/00159816:_____/23:00079276 - isvavai.cz</a>
Výsledek na webu
<a href="https://link.springer.com/article/10.1007/s11756-023-01539-8" target="_blank" >https://link.springer.com/article/10.1007/s11756-023-01539-8</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s11756-023-01539-8" target="_blank" >10.1007/s11756-023-01539-8</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Recombinant production of human antimicrobial peptide LL-37 and its secondary structure
Popis výsledku v původním jazyce
Antimicrobial peptides, including the human cathelicidin LL-37, offer a possible solution to the global problem of bacterial resistance to antibiotics. LL-37 peptide has potent antimicrobial effects against current multi-drug resistant bacterial strains. The peptide itself is also characterized by a very diverse range of immunomodulatory effects. The aim of this study was to produce antimicrobially active peptide LL-37 in E. coli in high yields using an own expression system pUbEx100 with the fusion protein ubiquitin. The results showed that the peptide GLL-37 could be produced in high amounts, but this peptide did not have antimicrobial activity compared to synthetically produced LL-37. CD spectroscopy results showed that the produced peptide GLL-37 is in alpha-helix form in contrast to the sLL-37 (random-coil form). The recombinant peptide GLL-37 can not bind to the membrane in the alpha-helix form, it would have to be in the form of a random-coil. This study confirms by CD spectroscopy the previously observed mechanism of access of LL-37 peptide to the bacterial membrane obtained by NMR.
Název v anglickém jazyce
Recombinant production of human antimicrobial peptide LL-37 and its secondary structure
Popis výsledku anglicky
Antimicrobial peptides, including the human cathelicidin LL-37, offer a possible solution to the global problem of bacterial resistance to antibiotics. LL-37 peptide has potent antimicrobial effects against current multi-drug resistant bacterial strains. The peptide itself is also characterized by a very diverse range of immunomodulatory effects. The aim of this study was to produce antimicrobially active peptide LL-37 in E. coli in high yields using an own expression system pUbEx100 with the fusion protein ubiquitin. The results showed that the peptide GLL-37 could be produced in high amounts, but this peptide did not have antimicrobial activity compared to synthetically produced LL-37. CD spectroscopy results showed that the produced peptide GLL-37 is in alpha-helix form in contrast to the sLL-37 (random-coil form). The recombinant peptide GLL-37 can not bind to the membrane in the alpha-helix form, it would have to be in the form of a random-coil. This study confirms by CD spectroscopy the previously observed mechanism of access of LL-37 peptide to the bacterial membrane obtained by NMR.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10602 - Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2023
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biologia
ISSN
0006-3088
e-ISSN
1336-9563
Svazek periodika
79
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
SK - Slovenská republika
Počet stran výsledku
11
Strana od-do
263-273
Kód UT WoS článku
001076907300002
EID výsledku v databázi Scopus
—