INVESTIGATIONS INTO THE ABILITY OF THE PEPTIDE, HAL18, TO INTERACT WITH BACTERIAL MEMBRANES
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SCOPUS
- Title
- INVESTIGATIONS INTO THE ABILITY OF THE PEPTIDE, HAL18, TO INTERACT WITH BACTERIAL MEMBRANES
- Authors
- Dennison, SR; Kim, YS; Cha, HJ; Phoenix, DA
- Date Issued
- 2008-11
- Publisher
- SPRINGER
- Abstract
- Halocidin was isolated from hemocytes, Halocynthia aurantium as a heterodimeric peptide consisting of two alpha-helical subunits, Hal15 and Hal18. Hal18 was shown to have antibacterial properties against Bacillus subtilis (MLC = 15 mu M) and Escherichia coli (MLC = 100 mu M). The peptide was shown to produce stable monolayers, which were characteristic of alpha-helical peptides predicted to orientate parallel to the surface of the interface. Constant area assays showed that Hal18 was surface active (4 mu M) inducing surface pressure changes > 30 mN m(-1) characteristic of membrane interactive peptides. The peptide induced stable surface pressure changes in monolayers that were mimetic of B. subtilis membranes (circa 7 mN m(-1)) and E. coli membrane-mimics (circa 4 mN m(-1)). Hal18 inserted readily into zwitterionic DOPE and anionic DOPG monolayers inducing surface pressure changes circa 8 mN m(-1) in both cases, providing evidence that interaction is not headgroup specific. Thermodynamic analysis of compression isotherms showed that the presence of Hal18 destabilised B. subtilis membranes (Delta G (Mix) > 0), which is in contrast to its stabilising effect on E. coli lipid extract implying the differential antimicrobial efficacy may be driven by lipid packing.
- Keywords
- Antimicrobial peptide; Monolayer stability; Peptide monolayer; Lipid-peptide interactions; Thermodynamic analysis; ORIENTATED ALPHA-HELICES; ANTIMICROBIAL PEPTIDES; LIPID MONOLAYERS; TILTED PEPTIDES; DESTABILIZATION; PURIFICATION; PACKING; BINDING
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/29381
- DOI
- 10.1007/s00249-008-0352-6
- ISSN
- 0175-7571
- Article Type
- Article
- Citation
- EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, vol. 38, no. 1, page. 37 - 43, 2008-11
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