Code for collagen's stability deciphered

  title={Code for collagen's stability deciphered},
  author={Steven K. Holmgren and Kimberly M. Taylor and Lynn E. Bretscher and Ronald T. Raines},
The most abundant protein in animals is collagen. In connective tissue, this protein is present as chains wound in tight triple helices which are organized into fibrils of great tensile strength and thermal stability,. We propose a new explanation for this stability. 
Collagen structure and stability.
The fibrillar structure of type I collagen-the prototypical collagen fibril-has been revealed in detail and will guide further development of artificial collagenous materials for biomedicine and nanotechnology.
Stronger and Longer Synthetic Collagen
Collagen is the most abundant protein in the human proteome. The post-translational modification of collagen by the enzyme prolyl 4-hydroxylase increases markedly the conformational stability of the
Emil Thomas Kaiser Award
Collagen is the most abundant protein in animals. The conformational stability of the collagen triple helix is enhanced by the hydroxyl group of its prevalent (2S,4R)-4-hydroxyproline residues. For
The stereoelectronic basis of collagen stability
We conclude that collagen stability does not rely on bridging water molecules. Rather, stereoelectronic effects preorganize collagen strands. Specifically, an electronegative substituent in the 4(R)
Insights on the conformational stability of collagen.
Much work has been done on synthetic mimics of collagen that contain host-guest peptides, tethers, peptoid residues, or analogs of the prevalent 4(R)-hydroxy-L-proline residues that reveal much about the chemical basis for collagen stability, and could spawn useful new biomaterials.
2005 Emil Thomas Kaiser Award
  • R. Raines
  • Chemistry, Medicine
    Protein science : a publication of the Protein Society
  • 2006
This work tested the hypothesis that the conformational stability of the collagen triple helix is enhanced by the hydroxyl group of its prevalent (2S,4R)‐4‐hydroxyproline residues and unveiled a wealth of stereoelectronic effects that contribute markedly to the stability of collagen, as well as other proteins.
Modulating the conformational stability of triple-helical collagen by chemical modification
The conformational stability of triple helical (ProHypGly)10 can be altered by chemical modification of the Hyp hydroxyl group.
Peptides that anneal to natural collagen in vitro and ex vivo.
It is shown that CMPs containing 4-fluoroproline residues, in particular, bind tightly to mammalian collagen in vitro and to a mouse wound ex vivo, which could herald a new era in assessing or treating wounds.
Characterization of collagen‐like heterotrimers: Implications for triple‐helix stability
The effects of proline hydroxylation on collagen triple‐helix stability, an issue that is still under discussion, is dealt with.
Cyclic Peptide Mimetic of Damaged Collagen
This cyclic peptide enables the assessment of CMPs for utility in annealing to damaged collagen and has potential use in the diagnosis and treatment of fibrotic diseases and wounds.