2N8D

In silico designed antimicrobial peptide Lavracin

2N8D の概要

• エントリーDOI: 10.2210/pdb2n8d/pdb
• NMR情報: BMRB: 25846
• 分子名称: antimicrobial peptide Lavracin (1 entity in total)
• 機能のキーワード: de novo protein, antimicrobial peptide
• 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: 2249.72

構造登録者

Pillong, M.,Blatter, M.,Schneider, G. (登録日: 2015-10-13, 公開日: 2017-01-18, 最終更新日: 2024-11-06)

主引用文献

Pillong, M.,Hiss, J.A.,Schneider, P.,Lin, Y.C.,Posselt, G.,Pfeiffer, B.,Blatter, M.,Muller, A.T.,Bachler, S.,Neuhaus, C.S.,Dittrich, P.S.,Altmann, K.H.,Wessler, S.,Schneider, G.
Rational Design of Membrane-Pore-Forming Peptides.
Small, 13:-, 2017

PubMed Abstract: Specific interactions of peptides with lipid membranes are essential for cellular communication and constitute a central aspect of the innate host defense against pathogens. A computational method for generating innovative membrane-pore-forming peptides inspired by natural templates is presented. Peptide representation in terms of sequence- and topology-dependent hydrophobic moments is introduced. This design concept proves to be appropriate for the de novo generation of first-in-class membrane-active peptides with the anticipated mode of action. The designed peptides outperform the natural template in terms of their antibacterial activity. They form a kinked helical structure and self-assemble in the membrane by an entropy-driven mechanism to form dynamically growing pores that are dependent on the lipid composition. The results of this study demonstrate the unique potential of natural template-based peptide design for chemical biology and medicinal chemistry.

PubMed: 28799716
DOI: 10.1002/smll.201701316

実験手法

SOLUTION NMR