Understanding Bioavailability of Peptides
TAGS: Nature, Global Health, Life Sciences, Food/Agriculture, Chemistry, Theoretical-licensing
AWARD: $20,000 USD | DEADLINE: 1/09/13 | ACTIVE SOLVERS: 35 | POSTED: 11/09/12
What sequence and structural factors influence the bioavailability of small peptides following ingestion? Which physiological parameters determine whether peptides reach and persist in the systemic circulation, and which models would be relevant to assess peptide bioavailability? The Seeker is looking for insightful submissions that are supported by peer-reviewed publications, in-silico modelling &/or existing research data.
This Challenge requires only a written proposal.
Detailed Description & Requirements
Hydrolysed milk proteins are used both in infant feeds and other food products. Either heat and pH or enzymatic processes are used to hydrolyze whey or casein proteins to smaller peptide species or single amino acids. These preparations contain peptides of 2-12 amino acids in length.
While the mechanisms by which individual amino acids are absorbed and metabolized is well understood the knowledge about absorption mechanisms of peptides is much more limited. This Challenge requests in depth theoretical insights regarding which amino acid sequences or structures of casein-derived peptides and which physiological parameters are most influential in determining bioavailability. The focus is on bioavailability in human infants (0-2 years).
Bovine casein is a mix of AlphaS1, AlphaS2, Beta and Kappa-casein. Extensively hydrolysed casein contains a mixture of peptides 2-12 amino acids in length. Besides their established application in cow’s milk allergy, these casein hydrolysate derived peptides may [更多]