8IS3

Structural model for the micelle-bound indolicidin-like peptide in solution

8IS3 の概要

• エントリーDOI: 10.2210/pdb8is3/pdb
• 分子名称: Indolicidin-like antimicrobial peptide (1 entity in total)
• 機能のキーワード: antimicrobial peptide, indolicidin-like peptide, peptide structure, peptide-micelle interaction, nmr spectroscopy, antimicrobial protein
• 由来する生物種: Bos taurus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1302.59

構造登録者

Kim, B.,Ko, Y.H.,Kim, J.,Lee, J.,Nam, C.H.,Kim, J.H. (登録日: 2023-03-20, 公開日: 2024-03-20, 最終更新日: 2025-04-02)

主引用文献

Kim, J.,Lee, J.,Kang, E.,Lee, K.,Lee, K.,Cheon, Y.,Lee, S.,Kim, B.,Ko, Y.H.,Kim, J.H.,In, S.I.,Nam, C.H.
Insights into an indolicidin-derived low-toxic anti-microbial peptide's efficacy against bacterial cells while preserving eukaryotic cell viability.
Biofactors, 51:e2145-e2145, 2025

PubMed Abstract: Antimicrobial peptides (AMPs) are a current solution to combat antibiotic resistance, but they have limitations, including their expensive production process and the induction of cytotoxic effects. We have developed novel AMP candidate (peptide 3.1) based on indolicidin, among the shortest naturally occurring AMP. The antimicrobial activity of this peptide is demonstrated by the minimum inhibitory concentration, while the hemolysis tests and MTT assay indicate its low cytotoxicity. In optical diffraction tomography, red blood cells treated with peptide 3.1 showed no discernible effects, in contrast to indolicidin. However, peptide 3.1 did induce cell lysis in E. coli, leading to a reduced potential for the development of antibiotic resistance. To investigate the mechanism underlying membrane selectivity, the structure of peptide 3.1 was analyzed using nuclear magnetic resonance spectroscopy and molecular dynamics simulations. Peptide 3.1 is structured with an increased distinction between hydrophobic and charged residues and remained in close proximity to the eukaryotic membrane. On the other hand, peptide 3.1 exhibited a disordered conformation when approaching the prokaryotic membrane, similar to indolicidin, leading to its penetration into the membrane. Consequently, it appears that the amphipathicity and structural rigidity of peptide 3.1 contribute to its membrane selectivity. In conclusion, this study may lead to the development of Peptide 3.1, a promising commercial candidate based on its low cost to produce and low cytotoxicity. We have also shed light on the mechanism of action of AMP, which exhibits selective toxicity to bacteria while not damaging eukaryotic cells.

PubMed: 39569798
DOI: 10.1002/biof.2145

実験手法

SOLUTION NMR