A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers

Farid Sa'adedin; Jeremy P. Bradshaw

doi:10.2174/0929866511009011345

A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers

Farid Sa'adedin, Jeremy P. Bradshaw

Vice Chancellor's Office

University of Edinburgh

Research output: Contribution to journal › Article › peer-review

1 Citation (SciVal)

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
Pages (from-to)	1345-1350
Number of pages	6
Journal	Protein and Peptide Letters
Volume	17
Issue number	11
DOIs	https://doi.org/10.2174/0929866511009011345
Publication status	Published - 1 Jan 2010

Keywords

Amphipathic helix
Antimicrobial peptide
DSC
LS3
Phase transition
Phosphatidylethanolamine

ASJC Scopus subject areas

Structural Biology
Biochemistry

Access to Document

10.2174/0929866511009011345

Cite this

@article{4251fa5bc2c6477facdf6c50ee9ee8b8,

title = "A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers",

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.",

keywords = "Amphipathic helix, Antimicrobial peptide, DSC, LS3, Phase transition, Phosphatidylethanolamine",

author = "Farid Sa'adedin and Bradshaw, {Jeremy P.}",

year = "2010",

month = jan,

day = "1",

doi = "10.2174/0929866511009011345",

language = "English",

volume = "17",

pages = "1345--1350",

journal = "Protein and Peptide Letters",

issn = "0929-8665",

publisher = "Bentham Science Publishers",

number = "11",

}

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

AN - SCOPUS:78650633261

SN - 0929-8665

VL - 17

SP - 1345

EP - 1350

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 11

ER -

A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this