Abstract
Differential Scanning Calorimetry studies of a synthetic peptide revealed the peptide decreased the temperature of the lamellar-hexagonal phase transition of cis-trans mixtures of phosphatidylethanolamine. The transition enthalpy varied significantly with lipid composition. The findings are discussed with reference to peptide saturation on the bilayer surface, bilayer thinning and peptide orientation.
Original language | English |
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Pages (from-to) | 1345-1350 |
Number of pages | 6 |
Journal | Protein and Peptide Letters |
Volume | 17 |
Issue number | 11 |
DOIs | |
Publication status | Published - 1 Jan 2010 |
Keywords
- Amphipathic helix
- Antimicrobial peptide
- DSC
- LS3
- Phase transition
- Phosphatidylethanolamine
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
Cite this
A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers. / Sa'adedin, Farid; Bradshaw, Jeremy P.
In: Protein and Peptide Letters, Vol. 17, No. 11, 01.01.2010, p. 1345-1350.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers
AU - Sa'adedin, Farid
AU - Bradshaw, Jeremy P.
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Differential Scanning Calorimetry studies of a synthetic peptide revealed the peptide decreased the temperature of the lamellar-hexagonal phase transition of cis-trans mixtures of phosphatidylethanolamine. The transition enthalpy varied significantly with lipid composition. The findings are discussed with reference to peptide saturation on the bilayer surface, bilayer thinning and peptide orientation.
AB - Differential Scanning Calorimetry studies of a synthetic peptide revealed the peptide decreased the temperature of the lamellar-hexagonal phase transition of cis-trans mixtures of phosphatidylethanolamine. The transition enthalpy varied significantly with lipid composition. The findings are discussed with reference to peptide saturation on the bilayer surface, bilayer thinning and peptide orientation.
KW - Amphipathic helix
KW - Antimicrobial peptide
KW - DSC
KW - LS3
KW - Phase transition
KW - Phosphatidylethanolamine
UR - http://www.scopus.com/inward/record.url?scp=78650633261&partnerID=8YFLogxK
U2 - 10.2174/0929866511009011345
DO - 10.2174/0929866511009011345
M3 - Article
VL - 17
SP - 1345
EP - 1350
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
SN - 0929-8665
IS - 11
ER -