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 id entification of peptides showing new binding specificity. This technol ogy was applied to the isolation of peptides binding to HIV-1 nucleoca psid protein (NCp7). Three different prolin reach peptide sequences, i nteracting with NCp7, mere isolated, from a constrained phage displaye d-peptide library of 10(8) independent clones. The three peptide seque nces, isolated from the peptide library, mere shown to bind NCp7 in th e region 30-52. Moreover, two of them share the PP-(D/E)R consensus se quence.