期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 70, 期 47, 页码 14947-14958出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.2c05024
关键词
casein; sleep-enhancing peptides; pharmacokinetics; quantum mechanics; structure-activity relationship
资金
- Guangdong Provincial Key RD Programme
- National Natural Science Foundation of China
- Notes
- [2022B0202030001]
- [32172134]
YPVEPF, an outstanding sleep-enhancing peptide derived from casein, shows instability against gastrointestinal enzymes but can be detected in vivo with strong sleep-enhancing effects. The N-terminus Tyr plays a dominant role in YPVEPF.
YPVEPF (Tyr-Pro-Val-Glu-Pro-Phe) is an outstanding sleep-enhancing peptide derived from casein. This study aimed to evaluate the bioavailability of YPVEPF in vitro and in vivo and to explore its structure-activity relationship through a sleep test and cheminformatics. Our results showed that YPVEPF was unstable against gastrointestinal enzymes and almost totally degraded to YPVEP in vitro. However, the pharmaco-kinetics results in vivo showed that the C-max of YPVEPF was 10.38 +/- 4.01 ng/mL at 5 min, and YPVEPF could be detected in the stomach, intestine, and brain at 12.89 +/- 0.55, 10.26 +/- 0.23, and 2.47 +/- 0.55 ng/g, respectively. The main metabolites including YPVEP, YP, PVEPF, and PVEP were identified. We first explored whether the fragment YPVEP also had a strong sleep-enhancing effect, and the sleep-enhancing effects of PVEPF and PVEP (lacking a Tyr residue) significantly decreased compared with those of YPVEPF and YPVEP. Moreover, molecular docking and quantum calculations revealed that the N-terminus Tyr played a dominant role in YPVEPF and YPVEP. They had distinctive self-folding structures and varying electron-withdrawing properties of the groups at the N terminus, allowing different binding modes and electron/proton transfer.
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