ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated.
If you have any questions, please contact Marianne Reed at mreed@ku.edu .
Solution Structure of A Novel T-cell Adhesion Inhibitor Derived from the Fragment of ICAM-1 Receptor: Cyclo(1,8)-Cys-Pro-ArgGly-Gly-Ser-Val-Cys
dc.contributor.author | Tejo, Bimo A. | |
dc.contributor.author | Siahaan, Teruna J. | |
dc.date.accessioned | 2017-05-09T18:19:48Z | |
dc.date.available | 2017-05-09T18:19:48Z | |
dc.date.issued | 2009-08 | |
dc.identifier.citation | Tejo, B. A., & Siahaan, T. J. (2009). Solution Structure of A Novel T-cell Adhesion Inhibitor Derived from the Fragment of ICAM-1 Receptor: Cyclo(1,8)-Cys-Pro-Arg-Gly-Gly-Ser-Val-Cys. Biopolymers, 91(8), 633–641. http://doi.org/10.1002/bip.21192 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24047 | |
dc.description | This is the peer reviewed version of the following article: Tejo, B. A., & Siahaan, T. J. (2009). Solution Structure of A Novel T-cell Adhesion Inhibitor Derived from the Fragment of ICAM-1 Receptor: Cyclo(1,8)-Cys-Pro-Arg-Gly-Gly-Ser-Val-Cys. Biopolymers, 91(8), 633–641. http://doi.org/10.1002/bip.21192, which has been published in final form at doi.org/10.1002/bip.21192. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving | en_US |
dc.description.abstract | This study is aimed at elucidating the structure of a novel T-cell adhesion inhibitor, cyclo(1,8)-CPRGGSVC using one- and two-dimensional 1H NMR and molecular dynamics (MD) simulation. The peptide is derived from the sequence of its parent peptide cIBR (cyclo(1,12)-PenPRGGSVLVTGC), which is a fragment of intercellular adhesion molecule-1 (ICAM-1). Our previous results show that the cyclo(1,8)-CPRGGSVC peptide binds to the LFA-1 I-domain and inhibits heterotypic T-cell adhesion, presumably by blocking the LFA-1/ICAM-1 interactions. The structure of the peptide was determined using NMR and MD simulation in aqueous solution. Our results indicate that the peptide adopts type-I β-turn conformation at the Pro2-Arg3-Gly4-Gly5 (PRGG) sequence. The β-turn structure at the PRGG motif is well conserved in cIBR peptide and ICAM-1 receptor, which suggests the importance of the PRGG motif for the biological activity of cyclo(1,8)-CPRGGSVC peptide. Meanwhile, the Gly5-Ser6-Val7-Cys8-Cys1 (GSVCC) sequence forms a “turn-like” random coil structure that does not belong to any structured motif. Therefore, cyclo(1,8)-CPRGGSVC peptide has only one structured region at the PRGG sequence, which may play an important role in the binding of the peptide to the LFA-1 I-domain. The conserved β-turn conformation of the PRGG motif in ICAM-1, cIBR, and cyclo(1,8)-CPRGGSVC peptides can potentially be used to design peptidomimetics. | en_US |
dc.publisher | Wiley | en_US |
dc.rights | © 2009 Wiley Periodicals, Inc. | en_US |
dc.subject | Autoimmune diseases | en_US |
dc.subject | β-turn | en_US |
dc.subject | ICAM-1 | en_US |
dc.subject | LFA-1 | en_US |
dc.subject | T-cell adhesion | en_US |
dc.title | Solution Structure of A Novel T-cell Adhesion Inhibitor Derived from the Fragment of ICAM-1 Receptor: Cyclo(1,8)-Cys-Pro-ArgGly-Gly-Ser-Val-Cys | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Tejo, Bimo A. | |
kusw.kuauthor | Siahaan, Teruna J. | |
kusw.kudepartment | Pharmaceutical Chemistry | en_US |
dc.identifier.doi | 10.1002/bip.21192 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC2742958 | en_US |
dc.rights.accessrights | openAccess |