2MJS

Anoplin R5K T8W in DPC micelles

Summary for 2MJS

• Entry DOI: 10.2210/pdb2mjs/pdb
• Related: 2MJQ 2MJR 2MJT
• NMR Information: BMRB: 11553
• Descriptor: Anoplin, UNKNOWN ATOM OR ION, dodecyl 2-(trimethylammonio)ethyl phosphate (3 entities in total)
• Functional Keywords: amphipathic helix, antimicrobial protein
• Biological source: Anoplius samariensis (Solitary wasp)
• Cellular location: Secreted: P0C005
• Total number of polymer chains: 1
• Total formula weight: 24057.64

Authors

Uggerhoej, L.,Poulsen, T.J.,Wimmer, R. (deposition date: 2014-01-16, release date: 2014-12-03, Last modification date: 2024-11-20)

Primary citation

Uggerhj, L.E.,Poulsen, T.J.,Munk, J.K.,Fredborg, M.,Sondergaard, T.E.,Frimodt-Moller, N.,Hansen, P.R.,Wimmer, R.
Rational Design of Alpha-Helical Antimicrobial Peptides: Do's and Don'ts.
Chembiochem, 16:242-253, 2015

PubMed Abstract: Antimicrobial peptides (AMPs) are promising candidates for battling multiresistant bacteria. Despite extensive research, structure-activity relationships of AMPs are not fully understood, and there is a lack of structural data relating to AMPs in lipids. Here we present the NMR structure of anoplin (GLLKRIKTLL-NH2 ) in a micellar environment. A vast library of substitutions was designed and tested for antimicrobial and hemolytic activity, as well as for changes in structure and lipid interactions. This showed that improvement of antimicrobial activity without concomitant introduction of strong hemolytic activity can be achieved through subtle increases in the hydrophobicity of the hydrophobic face or through subtle increases in the polarity of the hydrophilic face of the helix, or-most efficiently-a combination of both. A set of guidelines based on the results is given, for assistance in how to modify cationic α-helical AMPs in order to control activity and selectivity. The guidelines are finally tested on a different peptide.

PubMed: 25530580
DOI: 10.1002/cbic.201402581

Experimental method

SOLUTION NMR