Hydroxyproline-free Single Composition ABC Collagen Heterotrimer

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dc.citation.firstpage6014en_US
dc.citation.issueNumber16en_US
dc.citation.journalTitleJournal of the American Chemical Societyen_US
dc.citation.lastpage6017en_US
dc.citation.volumeNumber135en_US
dc.contributor.authorJalan, Abhishek A.en_US
dc.contributor.authorDemeler, Borriesen_US
dc.contributor.authorHartgerink, Jeffrey D.en_US
dc.date.accessioned2014-10-06T17:18:00Zen_US
dc.date.available2014-10-06T17:18:00Zen_US
dc.date.issued2013en_US
dc.description.abstractHydroxyproline plays a major role in stabilizing collagenous domains in eukaryotic organisms. Lack of this modification is associated with significant lowering in thermal stability of the collagen triple helix and may also affect fibrillogenesis and folding of the peptide chains. In contrast, even though bacterial collagens lack hydroxyproline, their thermal stability is comparable to fibrillar collagen. This has been attributed to the high frequency of charged amino acids found in bacterial collagen. Here we report a thermally stable hydroxyproline-free ABC heterotrimeric collagen mimetic system composed of decapositive and decanegative peptides and a zwitterionic peptide. None of the peptides contain hydroxyproline and furthermore the zwitterionic peptide does not even contain proline. The heterotrimer is electrostatically stabilized via multiple interpeptide lysine-aspartate and lysine-glutamate salt-bridges and maintains good thermal stability with a melting temperature of 37 °C. The ternary peptide mixture also populates a single composition ABC heterotrimer as confirmed by circular dichroism (CD) and Nuclear Magnetic Resonance (NMR) spectroscopy. This system illustrates the power of axial salt-bridges to direct and stabilize the self-assembly of a triple helix and may be useful in analogous designs in expression systems where the incorporation of hydroxyproline is challenging.en_US
dc.identifier.citationJalan, Abhishek A., Demeler, Borries and Hartgerink, Jeffrey D.. "Hydroxyproline-free Single Composition ABC Collagen Heterotrimer." <i>Journal of the American Chemical Society,</i> 135, no. 16 (2013) American Chemical Society: 6014-6017. http://dx.doi.org/10.1021/ja402187t.en_US
dc.identifier.doihttp://dx.doi.org/10.1021/ja402187ten_US
dc.identifier.urihttps://hdl.handle.net/1911/77396en_US
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by the American Chemical Society.en_US
dc.titleHydroxyproline-free Single Composition ABC Collagen Heterotrimeren_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
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