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https://hdl.handle.net/10356/94527
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. | URI: | https://hdl.handle.net/10356/94527 http://hdl.handle.net/10220/7477 |
DOI: | 10.1021/jm8008212 | Schools: | School of Biological Sciences | Rights: | © 2009 American Chemical Society. | Fulltext Permission: | none | Fulltext Availability: | No Fulltext |
Appears in Collections: | SBS Journal Articles |
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