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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