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Updated: Jul 14, 2026
Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide
Thomas Stangler1, Tuyen Tran, Silke Hoffmann
1Institut für Physikalische Biologie and BMFZ, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse 1, D-40225 Düsseldorf, Germany.
Abstract:
We studied the interaction of the artificial 12-aa proline-rich peptide PD1 with the SH3 domain of the hematopoietic cell kinase Hck and the peptide's potency in competitively displacing HIV-1 Nef from the Hck SH3 domain. PD1 was obtained from a phage display screen and exhibits exceptional affinity for the Hck SH3 domain (K(d)=0.23 microM). Competition experiments using NMR spectroscopy demonstrate that the peptide even displaces Nef from Hck SH3 and allow for estimation of the Nef-Hck SH3 dissociation constant (K(d)=0.44 microM), the strongest SH3 ligand interaction known so far. Consequences of this study for novel antiviral concepts are discussed.
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