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RP2E INRA Université de Lorraine

Interaction between dietary bioactive peptides of short length and bile salts in submicellar or micellar state

Food Chemistry, 209 (-), pp.114-122.

Guerin, J., Kriznik, A., Ramalanjaona, N., Le Roux, Y., Girardet, J.-M.

2016

Bile salts act as steroidal detergents in the gut, which could also interact with peptides and improve their bioavailability, but according to an unclear mechanism. The occurrence of direct interaction  between milk bioactive peptides, Ile-Asn-Tyr-Trp, Leu-Asp-Gln-Trp, and Leu-Gln-Lys-Trp, and different bile salts in submicellar or micellar state was investigated by intrinsic fluorescence measurement and dynamic light scattering, above the critical micellar concentration, the latter being determined by isothermal titration calorimetry. The peptides form aggregates, spontaneously. In the presence of bile salts, some released peptide monomers were bound at the micellar surface. The lack of hydrogen bond involving the C12-OH group of the steroid skeleton and the acidic function of some bile salts might promote the interaction with the peptides, as well as the lack of the C12-OH group rather than that of the C7-OH group. At submicellar concentrations, sodium taurochenodeoxycholate and taurodeoxycholate readily interacted with the most hydrophobic peptide Ile-Asn-Tyr-Trp.

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