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 .

Show simple item record

dc.contributor.authorTejo, Bimo A.
dc.contributor.authorSiahaan, Teruna J.
dc.date.accessioned2017-05-09T18:19:48Z
dc.date.available2017-05-09T18:19:48Z
dc.date.issued2009-08
dc.identifier.citationTejo, 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.21192en_US
dc.identifier.urihttp://hdl.handle.net/1808/24047
dc.descriptionThis 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-Archivingen_US
dc.description.abstractThis 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.publisherWileyen_US
dc.rights© 2009 Wiley Periodicals, Inc.en_US
dc.subjectAutoimmune diseasesen_US
dc.subjectβ-turnen_US
dc.subjectICAM-1en_US
dc.subjectLFA-1en_US
dc.subjectT-cell adhesionen_US
dc.titleSolution 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-Cysen_US
dc.typeArticleen_US
kusw.kuauthorTejo, Bimo A.
kusw.kuauthorSiahaan, Teruna J.
kusw.kudepartmentPharmaceutical Chemistryen_US
dc.identifier.doi10.1002/bip.21192en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC2742958en_US
dc.rights.accessrightsopenAccess


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record