Inhibition of ICAM-1/LFA-1-mediated heterotypic T-cell adhesion to epithelial cells: design of ICAM-1 cyclic peptides.
In this work, we have designed cyclic peptides (cIBL, cIBR, cIBC, CH4 and CH7) derived from the parent IB peptide (ICAM-1(1-21)) that are inhibitors of ICAM-1/LFA-1-mediated T-cell adhesion to Caco-2 cell monolayers. Cyclic peptide cIBR has the best activity of any of the peptides evaluated. The active ICAM-1 peptides have a common Pro-Arg-Gly sequence that may be important for binding to LFA-1.
Department of Pharmaceutical Chemistry, The University of Kansas, Simons Research Laboratories, 2095 Constant Avenue, Lawrence, KS 66047, USA.
Meagan E
ME
Anderson
Tatyana
T
Yakovleva
Yongbo
Y
Hu
Teruna J
TJ
Siahaan
D018938:Caco-2 Cells; D002448:Cell Adhesion / Q000502:physiology; D045744:Cell Line, Tumor; D004305:Dose-Response Relationship, Drug; D015195:Drug Design; D004847:Epithelial Cells / Q000502:physiology*; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000235:genetics / Q000378:metabolism*; D016169:Lymphocyte Function-Associated Antigen-1 / Q000235:genetics / Q000378:metabolism*; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000235:genetics / Q000378:metabolism*; D013601:T-Lymphocytes / Q000502:physiology*
D016169:Lymphocyte Function-Associated Antigen-1; D010456:Peptides, Cyclic; D018799:Intercellular Adhesion Molecule-1