Hydroxyproline-free Single Composition ABC Collagen Heterotrimer

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dc.citation.firstpage6014
dc.citation.issueNumber16
dc.citation.journalTitleJournal of the American Chemical Society
dc.citation.lastpage6017
dc.citation.volumeNumber135
dc.contributor.authorJalan, Abhishek A.
dc.contributor.authorDemeler, Borries
dc.contributor.authorHartgerink, Jeffrey D.
dc.date.accessioned2014-10-06T17:18:00Z
dc.date.available2014-10-06T17:18:00Z
dc.date.issued2013
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.
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.
dc.identifier.doihttp://dx.doi.org/10.1021/ja402187t
dc.identifier.urihttps://hdl.handle.net/1911/77396
dc.language.isoeng
dc.publisherAmerican Chemical Society
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.
dc.titleHydroxyproline-free Single Composition ABC Collagen Heterotrimer
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpost-print
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