Please use this identifier to cite or link to this item: https://doi.org/10.1021/cb400594q
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dc.titleEngineering the polyproline II propensity of a class II major histocompatibility complex ligand peptide
dc.contributor.authorUnudurthi, S.D.
dc.contributor.authorHotta, K.
dc.contributor.authorKim, C.-Y.
dc.date.accessioned2014-10-27T08:27:24Z
dc.date.available2014-10-27T08:27:24Z
dc.date.issued2013-11-15
dc.identifier.citationUnudurthi, S.D., Hotta, K., Kim, C.-Y. (2013-11-15). Engineering the polyproline II propensity of a class II major histocompatibility complex ligand peptide. ACS Chemical Biology 8 (11) : 2383-2387. ScholarBank@NUS Repository. https://doi.org/10.1021/cb400594q
dc.identifier.issn15548929
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100579
dc.description.abstractOur immune system constantly samples peptides found inside the body as a means to detect foreign pathogens, infected cells, and tumorous cells. T cells, which carry out the critical task of distinguishing self from nonself peptides, can only survey peptides that are presented by the major histocompatibility complex protein. We investigated how the secondary structure of a peptide, namely, the polyproline II helix content, influences major histocompatibility complex binding. We synthesized 12 analogues of the wheat gluten derived α-I-gliadin peptide and tested their binding to the celiac disease associated HLA-DQ2 protein. Our analogue library represents a broad spectrum of polyproline II propensities, ranging from random coil structure to high polyproline II helix content. Overall, there was no noticeable correlation between the peptide polyproline II helix content and HLA-DQ2 binding. One analogue peptide, which has low polyproline II helix content, showed a 4.5-fold superior binding compared to native α-I-gliadin. © 2013 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/cb400594q
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/cb400594q
dc.description.sourcetitleACS Chemical Biology
dc.description.volume8
dc.description.issue11
dc.description.page2383-2387
dc.description.codenACBCC
dc.identifier.isiut000327175300006
Appears in Collections:Staff Publications

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