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• W1989105663 abstract "Leukocyte 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." @default.
• W1989105663 created "2016-06-24" @default.
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• W1989105663 creator A5043937178 @default.
• W1989105663 date "2003-04-01" @default.
• W1989105663 modified "2023-10-18" @default.
• W1989105663 title "A Peptide Derived from LFA-1 Protein that Modulates T-cell Adhesion Binds to Soluble ICAM-1 Protein" @default.
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• W1989105663 doi "https://doi.org/10.1080/07391102.2003.10506880" @default.
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