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

J 2024

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

PAVELKA, Antonín, Lukáš VACEK, Adam NOREK, Šárka KOBZOVÁ, Lubomír JANDA et. al.

Základní údaje

Originální název

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

Autoři

PAVELKA, Antonín (203 Česká republika, domácí), Lukáš VACEK (203 Česká republika, domácí), Adam NOREK (203 Česká republika), Šárka KOBZOVÁ (203 Česká republika, domácí) a Lubomír JANDA (203 Česká republika, garant)

Vydání

Biologia, Springer, 2024, 0006-3088

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 1.500 v roce 2022

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1007/s11756-023-01539-8

UT WoS

001076907300002

Klíčová slova anglicky

LL-37; Secondary structure; Antibacterial activity; CD spectroscopy; GLL-37; Peptide

Štítky

14110113

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 30. 1. 2024 13:39, Mgr. Marie Šípková, DiS.

Anotace

V originále

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.

Návaznosti

NU22-05-00475, projekt VaV

Název: Léčba infekcí způsobených multirezistentními kmeny bakterií pomocí nových antibakteriálních přípravků založených na katelicidinových antimikrobiálních peptidech

Investor: Ministerstvo zdravotnictví ČR, Léčba infekcí způsobených multirezistentními kmeny bakterií pomocí nových antibakteriálních přípravků založených na katelicidinových antimikrobiálních peptidech, Podprogram 1 - standardní

Citovat

PAVELKA, Antonín, Lukáš VACEK, Adam NOREK, Šárka KOBZOVÁ a Lubomír JANDA. Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure. Biologia. Springer, 2024, roč. 79, č. 1, s. 263-273. ISSN 0006-3088. Dostupné z: https://dx.doi.org/10.1007/s11756-023-01539-8.

@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 a Lubomír JANDA. Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure. \textit{Biologia}. Springer, 2024, roč.~79, č.~1, s.~263-273. ISSN~0006-3088. Dostupné z: https://dx.doi.org/10.1007/s11756-023-01539-8.

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