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Use of a constrain phage displayed‐peptide library for the isolation of peptides binding to HIV‐1 nucleocapsid protein (NCp7)
Author(s) -
Lener D.,
Benarous R.,
Calogero R.A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00158-6
Subject(s) - peptide , peptide library , phage display , human immunodeficiency virus (hiv) , peptide sequence , isolation (microbiology) , chemistry , oligopeptide , biochemistry , microbiology and biotechnology , computational biology , biology , virology , bioinformatics , gene
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.