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" alpha-triple-helix peptides shows a pro-thrombotic activity compared to a scrambled negative control peptide which possesses no significant activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Blood Platelets / drug effects
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Circular Dichroism / methods
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Collagen Type III / chemical synthesis
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Collagen Type III / chemistry
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Collagen Type III / pharmacology*
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Drug Evaluation, Preclinical
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Humans
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Molecular Mimicry
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry
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Oligopeptides / pharmacology*
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Platelet Aggregation / drug effects*
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Platelet Aggregation Inhibitors / chemical synthesis
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Platelet Aggregation Inhibitors / chemistry
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Platelet Aggregation Inhibitors / pharmacology*
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Protein Conformation
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Protein Structure, Secondary
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Structure-Activity Relationship
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Thermodynamics
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Time Factors
Substances
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Collagen Type III
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Oligopeptides
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Platelet Aggregation Inhibitors