We described the antiviral activity of an octapeptide corresponding to a Trp-rich domain of feline immunodeficiency virus (FIV) transmembrane glycoprotein. To overcome the limited enzymatic stability of short peptides, the retroinverso analogue was prepared and tested for inhibitory activity of FIV in the presence or absence of normal cat serum. Differently from the unmodified peptide, the retroinverso analogue maintains strong inhibitory activity in serum. NMR studies showed that it displays crucial conformational features believed to be important for antiviral activity.
A retro-inverso analogue of the antiviral octapeptide C8 inhibits feline immunodeficiency virus in serum / A. M. DURSI; S. GIANNECCHINI; A. DI FENZA; C. ESPOSITO; A. CAROTENUTO; M. BENDINELLI; P. ROVERO. - In: JOURNAL OF MEDICINAL CHEMISTRY. - ISSN 0022-2623. - STAMPA. - 46:(2003), pp. 1807-1810. [10.1021/jm034012h]
A retro-inverso analogue of the antiviral octapeptide C8 inhibits feline immunodeficiency virus in serum.
GIANNECCHINI, SIMONE;ROVERO, PAOLO
2003
Abstract
We described the antiviral activity of an octapeptide corresponding to a Trp-rich domain of feline immunodeficiency virus (FIV) transmembrane glycoprotein. To overcome the limited enzymatic stability of short peptides, the retroinverso analogue was prepared and tested for inhibitory activity of FIV in the presence or absence of normal cat serum. Differently from the unmodified peptide, the retroinverso analogue maintains strong inhibitory activity in serum. NMR studies showed that it displays crucial conformational features believed to be important for antiviral activity.
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