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Title: Design of β-hairpin peptides for modulation of cell adhesion by β-turn constraint
Authors: Satyanarayanajois, Seetharama D.
Giddu, Sumana
Subramanian, Vivekanandan
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.
DOI: 10.1021/jm8008212
Rights: © 2009 American Chemical Society.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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