Design, structure and biological activity of beta-turn peptides of CD2 protein for inhibition of T-cell adhesion

European Journal of Biochemistry
Liu JiningSeetharama D S Jois

Abstract

The interaction between cell-adhesion molecules CD2 and CD58 is critical for an immune response. Modulation or inhibition of these interactions has been shown to be therapeutically useful. Synthetic 12-mer linear and cyclic peptides, and cyclic hexapeptides based on rat CD2 protein, were designed to modulate CD2-CD58 interaction. The synthetic peptides effectively blocked the interaction between CD2-CD58 proteins as demonstrated by antibody binding, E-rosetting and heterotypic adhesion assays. NMR and molecular modeling studies indicated that the synthetic cyclic peptides exhibit beta-turn structure in solution and closely mimic the beta-turn structure of the surface epitopes of the CD2 protein. Docking studies of CD2 peptides and CD58 protein revealed the possible binding sites of the cyclic peptides on CD58 protein. The designed cyclic peptides with beta-turn structure have the ability to modulate the CD2-CD58 interaction.

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Citations

Feb 8, 2006·FEBS Letters·Csaba Hetényi, David van der Spoel
Oct 29, 2018·Journal of Computer-aided Molecular Design·Laurence LeherteAdèle D Laurent
Mar 5, 2011·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Bijan Kumar Paul, Nikhil Guchhait
Dec 5, 2009·Journal of the American Chemical Society·Anirban BhuniaHans-Christian Siebert
Jan 7, 2009·Journal of Medicinal Chemistry·Sumana GidduSeetharama D Satyanarayanajois
Dec 8, 2009·Carbohydrate Research·Abolfazl BarzegarSaman Hosseini Ashtiani

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