Recombinant production of human antimicrobial peptide LL-37 and its secondary structure

Result code in 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>

Result on the web

<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>

Result language

angličtina

Original language name

Recombinant production of human antimicrobial peptide LL-37 and its secondary structure

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10602 - Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2023

Confidentiality

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

Name of the periodical

Biologia

ISSN

0006-3088

e-ISSN

1336-9563

Volume of the periodical

79

Issue of the periodical within the volume

1

Country of publishing house

SK - SLOVAKIA

Number of pages

11

Pages from-to

263-273

UT code for WoS article

001076907300002

EID of the result in the Scopus database

—