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dc.titleA peptide derived from LFA-1 protein that modulates T-cell adhesion binds to soluble ICAM-1 protein
dc.contributor.authorJois, S.D.S.
dc.contributor.authorSiahaan, T.J.
dc.identifier.citationJois, S.D.S.,Siahaan, T.J. (2003-04). A peptide derived from LFA-1 protein that modulates T-cell adhesion binds to soluble ICAM-1 protein. Journal of Biomolecular Structure and Dynamics 20 (5) : 635-644. ScholarBank@NUS Repository.
dc.description.abstractLeukocyte function associated antigen 1 (LFA-1) and intercellular adhesion molecule 1 (ICAM-1) have been shown to be critical for adhesion process and immune response. Modulation or inhibition of the interaction between LFA-1/ICAM-1 interactions can result in therapeutic effects. Our group and others have shown that peptides derived from ICAM-1 or LFA-1 inhibit adhesion in a homotypic T-cell adhesion assay. It is likely that the peptides derived from ICAM-1 bind to LFA-1 and peptides derived from LFA-1 bind to ICAM-1 and inhibit the adhesion interaction. However, there are no concrete experimental evidence to show that peptides bind to either LFA-1 or ICAM-1 and inhibit the adhesion. Using NMR, CD and docking studies we have shown that an LFA-1 derived peptide binds to soluble ICAM-1. Docking studies using "autodock" resulted in LFA-1 peptide interacting with the ICAM-1 protein near Glu34. The proposed model based on our experimental data indicated that the LFA-1 peptide interacts with the protein via three intermolecular hydrogen bonds. Hydrophobic interactions also play a role in stabilizing the complex.
dc.subjectCell adhesion inhibition
dc.subjectPeptide-protein complex
dc.description.sourcetitleJournal of Biomolecular Structure and Dynamics
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