6MK8

NMR structure of Database designed and improved anti-Staphylococcal peptide DFT503 bound to micelles

6MK8 の概要

• エントリーDOI: 10.2210/pdb6mk8/pdb
• NMR情報: BMRB: 30524
• 分子名称: Anti-Staphylococcal peptide DFT503 (1 entity in total)
• 機能のキーワード: antimicrobial peptides, amphipathic helix, leucine-rich peptides, database designed peptides, antimicrobial protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1338.72

構造登録者

Wang, G. (登録日: 2018-09-25, 公開日: 2019-06-19, 最終更新日: 2024-10-16)

主引用文献

Mishra, B.,Lakshmaiah Narayana, J.,Lushnikova, T.,Wang, X.,Wang, G.
Low cationicity is important for systemic in vivo efficacy of database-derived peptides against drug-resistant Gram-positive pathogens.
Proc.Natl.Acad.Sci.USA, 116:13517-13522, 2019

PubMed Abstract: As bacterial resistance to traditional antibiotics continues to emerge, new alternatives are urgently needed. Antimicrobial peptides (AMPs) are important candidates. However, how AMPs are designed with in vivo efficacy is poorly understood. Our study was designed to understand structural moieties of cationic peptides that would lead to their successful use as antibacterial agents. In contrast to the common perception, serum binding and peptide stability were not the major reasons for in vivo failure in our studies. Rather, our systematic study of a series of peptides with varying lysines revealed the significance of low cationicity for systemic in vivo efficacy against Gram-positive pathogens. We propose that peptides with biased amino acid compositions are not favored to associate with multiple host factors and are more likely to show in vivo efficacy. Thus, our results uncover a useful design strategy for developing potent peptides against multidrug-resistant pathogens.

PubMed: 31209048
DOI: 10.1073/pnas.1821410116

実験手法

SOLUTION NMR