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Volumn 8, Issue 10, 2013, Pages 1638-1642
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Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides
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Author keywords
helicity; Amphiphilicity; Antimicrobial peptides; Hemolytic activity; Hydrophobicity
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Indexed keywords
CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37;
PEPTIDE DERIVATIVE;
ANTIINFECTIVE AGENT;
ANTIMICROBIAL CATIONIC PEPTIDE;
ANTIBACTERIAL ACTIVITY;
ARTICLE;
CONTROLLED STUDY;
ESCHERICHIA COLI;
HEMOLYSIS;
HYDROPHOBICITY;
MEMBRANE DAMAGE;
MINIMUM INHIBITORY CONCENTRATION;
NONHUMAN;
PEPTIDE SYNTHESIS;
PRIORITY JOURNAL;
STAPHYLOCOCCUS AUREUS;
CHEMICAL PHENOMENA;
CHEMISTRY;
DRUG EFFECTS;
ERYTHROCYTE;
MICROBIAL SENSITIVITY TEST;
PROTEIN SECONDARY STRUCTURE;
ANTI-INFECTIVE AGENTS;
ANTIMICROBIAL CATIONIC PEPTIDES;
ERYTHROCYTES;
ESCHERICHIA COLI;
HEMOLYSIS;
HYDROPHOBIC AND HYDROPHILIC INTERACTIONS;
MICROBIAL SENSITIVITY TESTS;
PROTEIN STRUCTURE, SECONDARY;
STAPHYLOCOCCUS AUREUS;
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EID: 84884977014
PISSN: 18607179
EISSN: 18607187
Source Type: Journal
DOI: 10.1002/cmdc.201300264 Document Type: Article |
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Times cited : (20)
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References (24)
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