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Findings from Rice University Provides New Data about Extracellular Matrix Proteins (Rational Design of a Non-canonical "Sticky-Ended" Collagen...

July 1, 2014

Findings from Rice University Provides New Data about Extracellular Matrix Proteins (Rational Design of a Non-canonical "Sticky-Ended" Collagen Triple Helix)

By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Proteins. According to news reporting originating from Houston, Texas, by NewsRx correspondents, research stated, "In a canonical collagen triple helix, three peptides self-assemble into a supercoiled motif with a one-amino-acid offset between the peptide chains. Design of triple helices that contain more than one residue offset is lucrative, as it leaves the non-covalent interactions unsatisfied at the termini and renders the termini 'sticky' to further self-assemble into collagen-like nanofibers."

Our news editors obtained a quote from the research from Rice University, "Here we use lysine glutamate axial salt-bridges to design a heterotrimeric collagen triple helix, ABC-1, containing a non-canonical offset of four residues between the peptide chains. The four-residue offset is necessary to prevent aggregation, which would prevent characterization of the non-canonical chain arrangement at the molecular level by NMR spectroscopy. A second heterotrimer, ABC-2, also stabilized by axial salt-bridges, is designed containing a canonical one-amino-acid offset to facilitate comparison of structure and stability by CD and NMR ABC-1 and ABC-2 demonstrate our ability to modulate chain offset in a collagen triple helix."

According to the news editors, the research concluded: "This lays the groundwork to design longer, and therefore stickier, offsets allowing access to a new class of collagen-related nanostructures."

For more information on this research see: Rational Design of a Non-canonical "Sticky-Ended" Collagen Triple Helix. Journal of the American Chemical Society, 2014;136(21):7535-7538. Journal of the American Chemical Society can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society -; Journal of the American Chemical Society -

The news editors report that additional information may be obtained by contacting A.A. Jalan, Rice University, Dept. of Bioengn, Houston, TX 77005, United States. Additional authors for this research include K.A. Jochim and J.D. Hartgerink (see also Proteins).

Keywords for this news article include: Texas, Houston, Collagen, United States, North and Central America, Extracellular Matrix Proteins

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Source: Life Science Weekly

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