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

D Lener; R Benarous; R A Calogero

doi:10.1016/0014-5793(95)00158-6

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

FEBS Lett. 1995 Mar 13;361(1):85-8. doi: 10.1016/0014-5793(95)00158-6.

Authors

D Lener¹, R Benarous, R A Calogero

Affiliation

¹ Dipartimento di Genetica, Biologia Generale e Molecolare, Università di Napoli Federico II, Italy.

PMID: 7890046
DOI: 10.1016/0014-5793(95)00158-6

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.

MeSH terms

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

Substances

Capsid Proteins
Gene Products, gag
NCP7 protein, Human immunodeficiency virus 1
Peptides
Recombinant Fusion Proteins
Viral Proteins
gag Gene Products, Human Immunodeficiency Virus