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• W2007202906 abstract "Abstract: Leukocyte adherence mediated by intercellular adhesion molecule‐1 (ICAM‐1) binding to leukocyte function‐associated antigen (LFA‐1) is required for proper inflammatory and immune function. Inhibition of ICAM‐1LFA‐1 binding using monoclonal antibodies (mAb) has been shown to be efficacious at inhibiting lymphoma metastasis as well as leukocyte emigration into tissue in a number of inflammatory diseases such as ischemia−reperfusion injury, septic shock and rheumatoid arthritis. In this report, we describe the development and characterization of a small peptide antagonist of ICAM‐1‐dependent cell aggregation. By using repeated selection of a cyclic nonapeptide phage display library on purified ICAM‐1, we identified phage that were competitively eluted with anti‐ICAM‐1 mAb. The peptide sequences were determined by nucleotide sequencing, and the peptide sequence (C*LLRMRSIC*) (IP01) that occurred most frequently was chosen for further study. Phage expressing this peptide sequence specifically bound ICAM‐1 over a range of 5 × 10 6 to 1 × 10 8 phage/µL. A cyclic IP01 peptide, linear IP01 peptide, a cyclic nonapeptide with a scrambled IP01 sequence, and a random, cyclic nonapeptide were synthesized. The cyclic and linear IP01 peptides were able to inhibit ICAM‐1‐mediated cell aggregation at a concentration of 1 m m , whereas the random and scrambled peptide sequences did not alter aggregation. Cyclic IP01 had a half‐maximal inhibitory concentration of ≈ 970 µ m . Cyclic IP01 did not inhibit cellular aggregation that was dependent on ICAM‐2 or ICAM‐3. Alanine substitutions in the cyclic IP01 identified at least four amino acids necessary for inhibition of ICAM‐1 dependent cell aggregation; leucine 2, leucine 3, methionine 5, and arginine 6. Finally, we showed that cyclic IP01 can inhibit firm adhesion of neutrophils to endothelium, a critical event in inflammatory diseases, in an assay that recapitulates physiologic flow conditions. Homology of IP01 with the primary amino acid sequences of the α or β subunit of LFA‐1 was not identified. Thus, we identified a unique molecule that inhibits ICAM‐1 dependent cell adhesion, but is not related to the primary sequence of the ICAM‐1 ligand LFA‐1. Due to the small size and ability to block cell−cell adhesion, IP01 may serve as a useful tool for study of ICAM‐1 and LFA‐1 biology as well as for the development of small molecule therapeutics." @default.
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• W2007202906 date "2001-08-01" @default.
• W2007202906 modified "2023-10-18" @default.
• W2007202906 title "Novel cyclic peptide inhibits intercellular adhesion molecule-1-mediated cell aggregation" @default.
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• W2007202906 doi "https://doi.org/10.1034/j.1399-3011.2001.00899.x" @default.
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