A comparative study on the interactions of SMAP-29 with lipid monolayers.
This work investigates the discrimination of lipid monolayers by the ovine antimicrobial peptide SMAP-29 and compares it to that of the human LL-37 peptide. Fluid phospholipid monolayers were formed in a Langmuir trough and subsequently studied with the X-ray scattering techniques of X-ray reflectivity and grazing incidence X-ray diffraction. Any changes in the phospholipid structure after injection of peptide under the monolayer were considered to be due to interactions between the peptides and lipids. The data show that SMAP-29 discriminates against negatively charged phospholipids in a similar way to LL-37. However, it is even more interesting to note that despite a higher concentration of SMAP-29 near the monolayer, ensured by its greater charge as compared to LL-37, the amount of SMAP-29 needed to observe monolayer disruption was around three and a half times the number of molecules of LL-37 used to see similar changes with the same system. This result suggests that the structure, amino acid sequence or size of the peptide may well be as important as electrical charge and therefore gives many implications for the further study of antimicrobial peptides with regards to novel drug design and development.
School of Process, Environmental and Materials Engineering, University of Leeds, Leeds LS29JT, UK.
Frances
F
Neville
Andrey
A
Ivankin
Oleg
O
Konovalov
David
D
Gidalevitz
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D054804:Cathelicidins; D015195:Drug Design; D006801:Humans; D008055:Lipids / Q000737:chemistry*; D012756:Sheep; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D054804:Cathelicidins; D008055:Lipids; C403305:SMAP29 protein, Ovis aries; D014867:Water