In HIV-1 the nucleocapsid protein (NC) is essential in the virion assembly process. The discovery of substances able to interfere with the HIV-1 NC functions could be a starting point for the design of new drugs that might inhibit the HIV-1 viral infectivity. A single peptide sequence binding to the NC was isolated using a conformationally homogeneous phage displayed-peptide library. The minimal requirement for the NCp7/peptide interaction was the NCp7 region encompassing the second zinc finger.

Identification of a peptide binding to the HIV-1 nucleocapsid protein (NCP7) / Calogero, RAFFAELE ADOLFO; Lener, D.; Antico, G; DEL GAUDIO, Rosanna; Aulicino, A.; Geraci, Giuseppe. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - STAMPA. - 3:6(1996), pp. 377-383.

Identification of a peptide binding to the HIV-1 nucleocapsid protein (NCP7)

CALOGERO, RAFFAELE ADOLFO;DEL GAUDIO, ROSANNA;GERACI, GIUSEPPE
1996

Abstract

In HIV-1 the nucleocapsid protein (NC) is essential in the virion assembly process. The discovery of substances able to interfere with the HIV-1 NC functions could be a starting point for the design of new drugs that might inhibit the HIV-1 viral infectivity. A single peptide sequence binding to the NC was isolated using a conformationally homogeneous phage displayed-peptide library. The minimal requirement for the NCp7/peptide interaction was the NCp7 region encompassing the second zinc finger.
1996
Identification of a peptide binding to the HIV-1 nucleocapsid protein (NCP7) / Calogero, RAFFAELE ADOLFO; Lener, D.; Antico, G; DEL GAUDIO, Rosanna; Aulicino, A.; Geraci, Giuseppe. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - STAMPA. - 3:6(1996), pp. 377-383.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/475636
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