2. Academic Validation
  3. Structural analysis and mode of action of BMAP-27, a cathelicidin-derived antimicrobial peptide

Structural analysis and mode of action of BMAP-27, a cathelicidin-derived antimicrobial peptide

  • Peptides. 2019 Aug;118:170106. doi: 10.1016/j.peptides.2019.170106.
Sungtae Yang 1,  Chul Won Lee 2,  Hak Jun Kim 3,  Hyun-Ho Jung 4,  Jae Il Kim 4,  Song Yub Shin 5,  Sung-Heui Shin 6
Affiliations

Affiliations

  • 1 Department of Microbiology, Chosun University School of Medicine, Gwangju, 61452, South Korea. Electronic address: [email protected].
  • 2 Department of Chemistry, Chonnam National University, Gwangju, 61186, South Korea.
  • 3 Department of Chemistry, Pukyong National University, Busan, 48513, South Korea.
  • 4 School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, 61005, South Korea.
  • 5 Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, South Korea.
  • 6 Department of Microbiology, Chosun University School of Medicine, Gwangju, 61452, South Korea. Electronic address: [email protected].
PMID: 31226350 DOI: 10.1016/j.peptides.2019.170106
Abstract

BMAP-27, a member of cathelicidin family, plays an important role against Microorganisms, including bacteria and fungi. BMAP-27 may exert antimicrobial effects through membrane integrity disruption, but the exact molecular mechanism remains unclear. To identify the structural features important for antimicrobial activity and propose a mechanism underlying Antibacterial effects, we determined the nuclear magnetic resonance structure of BMAP-27 in a membrane-mimetic environment and investigated its interactions with lipid membranes. BMAP-27 exhibited a long N-terminal α-helix with faces patterned into aromatic and cationic regions, central kink, and short hydrophobic C-terminal helix. While the N-terminal 18-residue peptide (BMAP-18) exerted only Antibacterial activity, BMAP-27 showed potent activity against bacteria and Cancer cells. Both Peptides inhibited Bacterial growth, but BMAP-18 showed delayed bactericidal activity and BMAP-27 completely killed bacteria within 20 min. The differences in antimicrobial activities and microbicidal kinetics may be associated with membrane permeabilisation; BMAP-27 rapidly and largely disrupted membrane integrity, whereas BMAP-18 showed low membrane disruption activity. Thus, the N-terminal helix is sufficient to inhibit Bacterial growth and the C-terminal helix is involved in membrane permeabilisation for rapid bactericidal and efficient Anticancer activities. The structural and functional characterisation of BMAP-27 may encourage the development of novel antimicrobial/Anticancer agents.

Keywords

Aromatic cluster; BMAP-27; Bactericidal activity; Cathelicidin; Membrane depolarization; NMR structure; Peptide-membrane interaction.

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