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      Use of a constrain phage displayed-peptide library for the isolation of peptides binding to HIV-1 nucleocapsid protein (NCp7).

      Febs Letters
      Amino Acid Sequence, Bacteriophages, genetics, metabolism, Capsid, chemical synthesis, Capsid Proteins, Consensus Sequence, Gene Products, gag, HIV-1, Molecular Sequence Data, Peptides, Recombinant Fusion Proteins, Sequence Deletion, Sequence Homology, Amino Acid, Viral Proteins, Zinc Fingers, gag Gene Products, Human Immunodeficiency Virus

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          Abstract

          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.

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