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Volumn 1834, Issue 6, 2013, Pages 996-1002
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Novicidin's membrane permeabilizing activity is driven by membrane partitioning but not by helicity: A biophysical study of the impact of lipid charge and cholesterol
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Author keywords
Antimicrobial peptide; Equilibrium dialysis; Membrane permeabilization; Partitioning coefficient; Secondary structure; Thermodynamics of membrane binding
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Indexed keywords
CALCEIN;
CHOLESTEROL;
DIOLEOYLPHOSPHATIDYLCHOLINE;
DIOLEOYLPHOSPHATIDYLGLYCEROL;
LIPID;
NOVICIDIN;
PHOSPHOLIPID;
POLYPEPTIDE ANTIBIOTIC AGENT;
UNCLASSIFIED DRUG;
ARTICLE;
BIOPHYSICS;
CELL MEMBRANE PERMEABILITY;
CELL STRUCTURE;
CELL VACUOLE;
CIRCULAR DICHROISM;
CONTROLLED STUDY;
DRUG PROTEIN BINDING;
ENTHALPY;
ENTROPY;
EQUILIBRIUM DIALYSIS;
ISOTHERMAL TITRATION CALORIMETRY;
LIPID ANALYSIS;
LIPID BILAYER;
PHASE PARTITIONING;
PRIORITY JOURNAL;
PROTEIN SECONDARY STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
ANTIMICROBIAL CATIONIC PEPTIDES;
CHOLESTEROL;
CIRCULAR DICHROISM;
LIPID BILAYERS;
PERMEABILITY;
PHOSPHATIDYLCHOLINES;
PHOSPHOLIPIDS;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
THERMODYNAMICS;
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EID: 84878112718
PISSN: 15709639
EISSN: 18781454
Source Type: Journal
DOI: 10.1016/j.bbapap.2013.03.025 Document Type: Article |
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Times cited : (10)
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References (41)
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