Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides.

@article{Pentzien2008TransepithelialTA,
  title={Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides.},
  author={Anne-Kathrin Pentzien and H. -H. Meisel},
  journal={Zeitschrift fur Naturforschung. C, Journal of biosciences},
  year={2008},
  volume={63 5-6},
  pages={451-9}
}
The dipeptides Ala-Trp, Val-Phe, and Val-Tyr inhibit the angiotensin-I-converting enzyme. They are encrypted within the primary sequences of different food proteins, e.g. milk proteins. The angiotensin-I-converting enzyme inhibitory potency of these synthetic dipeptides was quantified using a spectrophotometric assay. The dipeptides showed no adverse effects on differentiated Caco-2 cells (model for human intestinal epithelium), as confirmed by transepithelial electrical resistance, microscopy… CONTINUE READING

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