Please use this identifier to cite or link to this item: https://doi.org/10.1111/j.1432-1033.2004.04198.x
Title: Design, structure and biological activity of β-turn peptides of CD2 protein for inhibition of T-cell adhesion
Authors: Jining, L.
Makagiansar, I.
Yusuf-Makagiansar, H.
Chow, V.T.K.
Siahaan, T.J.
Jois, S.D.S. 
Keywords: β-turn
CD2
Cyclic peptide
E-rosetting
LFA-3 (CD58)
Issue Date: Jul-2004
Citation: Jining, L., Makagiansar, I., Yusuf-Makagiansar, H., Chow, V.T.K., Siahaan, T.J., Jois, S.D.S. (2004-07). Design, structure and biological activity of β-turn peptides of CD2 protein for inhibition of T-cell adhesion. European Journal of Biochemistry 271 (14) : 2873-2886. ScholarBank@NUS Repository. https://doi.org/10.1111/j.1432-1033.2004.04198.x
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 β-turn structure in solution and closely mimic the β-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 β-turn structure have the ability to modulate the CD2-CD58 interaction.
Source Title: European Journal of Biochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/105797
ISSN: 00142956
DOI: 10.1111/j.1432-1033.2004.04198.x
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