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

Abstract

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.