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 | |