| PAVELKA, Antonín, Lukáš VACEK, Adam NOREK, Šárka KOBZOVÁ and Lubomír JANDA. Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure. Biologia. Springer, 2024, vol. 79, No 1, p. 263-273. ISSN 0006-3088. Available from: https://dx.doi.org/10.1007/s11756-023-01539-8. |
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@article{2320177,
author = {Pavelka, Antonín and Vacek, Lukáš and Norek, Adam and Kobzová, Šárka and Janda, Lubomír},
article_number = {1},
doi = {http://dx.doi.org/10.1007/s11756-023-01539-8},
keywords = {LL-37; Secondary structure; Antibacterial activity; CD spectroscopy; GLL-37; Peptide},
language = {eng},
issn = {0006-3088},
journal = {Biologia},
title = {Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure},
url = {https://link.springer.com/article/10.1007/s11756-023-01539-8},
volume = {79},
year = {2024}
}
TY - JOUR
ID - 2320177
AU - Pavelka, Antonín - Vacek, Lukáš - Norek, Adam - Kobzová, Šárka - Janda, Lubomír
PY - 2024
TI - Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure
JF - Biologia
VL - 79
IS - 1
SP - 263-273
EP - 263-273
PB - Springer
SN - 00063088
KW - LL-37
KW - Secondary structure
KW - Antibacterial activity
KW - CD spectroscopy
KW - GLL-37
KW - Peptide
UR - https://link.springer.com/article/10.1007/s11756-023-01539-8
N2 - 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 α-helix form in contrast to the sLL-37 (random-coil form). The recombinant peptide GLL-37 can not bind to the membrane in the α-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.
ER -
PAVELKA, Antonín, Lukáš VACEK, Adam NOREK, Šárka KOBZOVÁ and Lubomír JANDA. Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure. \textit{Biologia}. Springer, 2024, vol.~79, No~1, p.~263-273. ISSN~0006-3088. Available from: https://dx.doi.org/10.1007/s11756-023-01539-8.
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