Highly efficient macromolecule-sized poration of lipid bilayers by a synthetically evolved peptide

Journal of the American Chemical Society

Volumn 136, Issue 12, 2014, Pages 4724-4731

  Wiedman, Gregory ^b   Fuselier, Taylor ^a   He, Jing ^a   Searson, Peter C ^b   Hristova, Kalina ^b   Wimley, William C ^a  

^a TULANE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Johns Hopkins University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; LIPID BILAYERS; MACROMOLECULES;

BIOTECHNOLOGICAL APPLICATIONS; FUNCTIONAL CLASS; HIGH-THROUGHPUT SCREENS; LOW CONCENTRATIONS; MULTIPLE AREAS; PORE-FORMING PEPTIDES; SMALL MOLECULES; VESICLE MEMBRANES;

PEPTIDES;

ALAMETHICIN; BEE VENOM; CHYMOTRYPSIN; DEXTRAN; HEMOGLOBIN; MELITTIN; MELP5 PEPTIDE; STREPTAVIDIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; LIPID BILAYER;

ARTICLE; BILAYER MEMBRANE; CHANNEL GATING; COMPLEX FORMATION; CONTROLLED STUDY; ELECTROCHEMICAL IMPEDANCE SPECTROSCOPY; ERYTHROCYTE MEMBRANE; LIPID BILAYER; LIPID VESICLE; MACROMOLECULE; MEMBRANE CONDUCTANCE; MEMBRANE VESICLE; MOLECULAR EVOLUTION; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; POROSITY; PROTEIN SECONDARY STRUCTURE; SYNTHESIS;

AMINO ACID SEQUENCE; LIPID BILAYERS; MELITTEN; MOLECULAR SEQUENCE DATA; POROSITY; PROTEIN STRUCTURE, SECONDARY;

EID: 84897074288     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja500462s     Document Type: Article

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