Phage randomization in a charybdotoxin scaffold leads to CD4-mimetic recognition motifs that bind HIV-1 envelope through non-aromatic sequences

Journal of Peptide Research

Volumn 57, Issue 6, 2001, Pages 507-518

  Li, C ^a   Dowd, C S ^a   Zhang, W ^a,b   Chaiken, I M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b Sinogen Ltd   (China)

Author keywords

CD4; Charybdotoxin; gp120; HIV 1; Phage display

Indexed keywords

CD4 ANTIGEN; CHARYBDOTOXIN; GLYCOPROTEIN GP 120; T LYMPHOCYTE RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS; VIRUS ENVELOPE;

ANTIGENS, CD4; BASE SEQUENCE; BINDING SITES; CHARYBDOTOXIN; CHROMATOGRAPHY, AFFINITY; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; HIV ENVELOPE PROTEIN GP120; HIV-1; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDE LIBRARY; PEPTIDES;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; SCORPIONES;

EID: 0034966551     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1397-002X.2001.00876.x     Document Type: Article

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