| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1395067 | European Journal of Medicinal Chemistry | 2009 | 8 Pages |
Abstract
We report the synthesis of collagen related peptides containing the peptide sequence Lys-Hyp-Gly-Glu-Hyp-Gly-Pro-Lys. The anti-thrombotic activity effects of different glycine mutations in this sequence were studied in regard with their different adopted conformations. The biological results could be correlated to the glycine propensity to adopt a more stable polyproline II helix conformation. The incorporation of these sequences in “collagen-like” α-triple-helix peptides shows a pro-thrombotic activity compared to a scrambled negative control peptide which possesses no significant activity.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Julien Pêcher, Viviane Pires, Ibtissem Djaafri, Sophie Da Nascimento, Françoise Fauvel-Lafève, Chantal Legrand, Pascal Sonnet,