Bioavailability and bioavailable forms of collagen after oral administration to rats

J Agric Food Chem. 2015 Apr 15;63(14):3752-6. doi: 10.1021/jf5057502. Epub 2015 Apr 7.


The bioavailability and bioavailable forms of collagen after oral administration to rats were investigated in this study. The relative and absolute bioavailability of collagen were 57.8% and 49.6%, respectively, which was indirectly evaluated by the bioavailability of Hyp in collagen using a pharmacokinetic method. The amino acid profile of plasma showed that more than 63.4% of the collagen was absorbed from the intestine in the form of peptide, and there was a good linear correlation between the absorbed amount of an amino acid and its content in collagen (R(2) = 0.9225). The collagen peptides in plasma were purified by Sephadex G10 and Eclipse XDB C18 chromatography and further indentified (Ala-Asn, Ala-Hyp-Gly, Asp-Glu, Glu-Asn, Glu-Asp, Glu-Met, Gly-Pro-Hyp, Leu-Hyp, Leu-Met, Phe-Gly-Asn, Pro-Gly-Leu, Pro-Leu, Ser-Gly-Met, Ser-Hyp, Ser-Pro-Gly, Tyr-Met) with UPLC-ESI-MS. These results may help to speculate about the molecular mechanism behind the physiological effects of collagen after oral administration.

Keywords: bioavailability; bioavailable form; collagen; pepetide; pharmacokinetic.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Availability
  • Collagen / chemistry
  • Collagen / metabolism
  • Collagen / pharmacokinetics*
  • Female
  • Mass Spectrometry
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Rats
  • Rats, Sprague-Dawley


  • Peptide Fragments
  • Collagen