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.

Basic information

Original name

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

Authors

PAVELKA, Antonín (203 Czech Republic, belonging to the institution), Lukáš VACEK (203 Czech Republic, belonging to the institution), Adam NOREK (203 Czech Republic), Šárka KOBZOVÁ (203 Czech Republic, belonging to the institution) and Lubomír JANDA (203 Czech Republic, guarantor)

Edition

Biologia, Springer, 2024, 0006-3088

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 1.500 in 2022

Organization unit

Faculty of Science

DOI

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

UT WoS

001076907300002

Keywords in English

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

Abstract

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.

Links

NU22-05-00475, research and development project

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

Investor: Ministry of Health of the CR, Subprogram 1 - standard

Citovat

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.

@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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