Transmembrane segment peptides with double D-amino acid replacements: Helicity, hydrophobicity, and antimicrobial activity

Biopolymers - Peptide Science Section

Volumn 71, Issue 1, 2003, Pages 77-84

  Maeda, Mitsuko ^b   Melnyk, Roman A ^d   Partridge, Anthony W ^d   Liut, Li Ping ^c   Deber, Charles M ^a  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b KOBE GAKUIN UNIVERSITY   (Japan)

^c CTL ImmunoTherapies Corp   (United States)

^d NONE

Author keywords

Antimicrobial activity; CD; DD substitutions; Helicity; Hydrophobicity; Membrane insertion; Transmembrane peptides

Indexed keywords

CONFORMATIONS; ESCHERICHIA COLI; FLUORESCENCE; HYDROGEN BONDS; HYDROPHOBICITY; LIQUID CHROMATOGRAPHY; MUTAGENESIS; SPECTROSCOPIC ANALYSIS;

TRANSMEMBRANES;

POLYPEPTIDES;

DEXTRO AMINO ACID; LYSYLLYSLALANYLALANYLALANYLALANYLALANYLALANYLALANYLALANYLALANYLALANYLALANYL ALANYLTRYPTOPHYLALANYLALANYLALANYLALANYLALANYLALANYLLYSYLLYSYLLYSYLLYSINAMINE; MEMBRANE PROTEIN; PEPTIDE; PEPTIDE LIBRARY; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANTIMICROBIAL ACTIVITY; AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORESCENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROGEN BOND; HYDROPHOBICITY; MICELLE; MUTAGENESIS; PEPTIDE SYNTHESIS; PROTEIN CONFORMATION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; BINDING SITES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; DRUG DESIGN; ESCHERICHIA COLI; HYDROGEN BONDING; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; INSERTION SEQUENCES;

EID: 0038636490     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10383     Document Type: Article

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