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|Title:||Design of β-hairpin peptides for modulation of cell adhesion by β-turn constraint||Authors:||Satyanarayanajois, Seetharama D.
Yoon, Ho Sup
|Keywords:||DRNTU::Science::Biological sciences::Molecular biology||Issue Date:||2009||Source:||Giddu, S., Subramanian, V., Yoon, H. S., & Satyanarayanajois, S. D. (2009). Design of β-Hairpin Peptides for Modulation of Cell Adhesion by β-Turn Constraint. Journal of Medicinal Chemistry, 52(3), 726-736.||Series/Report no.:||Journal of medicinal Chemistry||Abstract:||The CD2−CD58 interaction in immune regulation and disease pathology has provided new targets for developing potential immunosuppressive agents. In the present study, we report the introduction of constraints to generate β-hairpin structures from the strand sequences of CD2 protein. The β-hairpin structures were induced in the designed peptides by introducing Pro-Gly sequences in the peptides. Results from NMR and MD simulation indicated that the peptides exhibited β-turn structure at the X-Pro-Gly-Y sequence and formed the β-hairpin structure in solution. The ability of these peptides to inhibit cell adhesion was evaluated by two cell adhesion assays. Among the peptides studied (1−4) (P1−P4), peptides 2−4 were able to inhibit cell adhesion between Jurkat cells and SRBC nearly 50% at 180 μM, and 80% inhibition between Jurkat cells and Caco-2 cells was seen at 90 μM. Peptide 1 did not show significant inhibition activity compared to control.||URI:||https://hdl.handle.net/10356/94527
|DOI:||10.1021/jm8008212||Rights:||© 2009 American Chemical Society.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||SBS Journal Articles|
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