A synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion

Proceedings of the National Academy of Sciences of the United States of America

Volumn 95, Issue 13, 1998, Pages 7287-7292

  Pritsker, Moshe ^a   Jones, Philip ^b   Blumenthal, Robert ^b   Shai, Yechiel ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 41;

AMINO ACID SEQUENCE; ARTICLE; CELL FUSION; CHIRALITY; ENANTIOMER; LIPID BILAYER; OLIGOMERIZATION; PEPTIDE SYNTHESIS; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SPECTROSCOPY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CELL MEMBRANE; CIRCULAR DICHROISM; GENE PRODUCTS, ENV; HIV ENVELOPE PROTEIN GP41; HIV-1; HIV-2; HUMANS; LIPID BILAYERS; LIPOSOMES; MEMBRANE FUSION; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PHOSPHATIDYLGLYCEROLS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0032560463     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.95.13.7287     Document Type: Article

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