2N8D

In silico designed antimicrobial peptide Lavracin

Summary for 2N8D

• Entry DOI: 10.2210/pdb2n8d/pdb
• NMR Information: BMRB: 25846
• Descriptor: antimicrobial peptide Lavracin (1 entity in total)
• Functional Keywords: de novo protein, antimicrobial peptide
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 2249.72

Authors

Pillong, M.,Blatter, M.,Schneider, G. (deposition date: 2015-10-13, release date: 2017-01-18, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

SOLUTION NMR