Use of a constrain phage displayed-peptide library for the isolation of peptides binding to HIV-1 nucleocapsid protein (NCp7).
It has been shown that peptide libraries are powerful tools for the identification of peptides showing new binding specificity. This technology was applied to the isolation of peptides binding to HIV-1 nucleocapsid protein (NCp7). Three different prolin reach peptide sequences, interacting with NCp7, were isolated, from a constrained phage displayed-peptide library of 10(8) independent clones. The three peptide sequences, isolated from the peptide library, were shown to bind NCp7 in the region 30-52. Moreover, two of them share the PP-(D/E)R consensus sequence.
Lener
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Dipartimento di Genetica, Biologia Generale e Molecolare, Università di Napoli Federico II, Italy.
Benarous
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Calogero
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RA
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics* / Q000378:metabolism; D002213:Capsid / Q000138:chemical synthesis / Q000378:metabolism*; D036022:Capsid Proteins; D016384:Consensus Sequence / Q000235:genetics; D015683:Gene Products, gag / Q000138:chemical synthesis / Q000378:metabolism*; D015497:HIV-1; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins; D016335:Zinc Fingers / Q000235:genetics; D054301:gag Gene Products, Human Immunodeficiency Virus
D036022:Capsid Proteins; D015683:Gene Products, gag; C071884:NCP7 protein, Human immunodeficiency virus 1; D010455:Peptides; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; D054301:gag Gene Products, Human Immunodeficiency Virus