Heterologous Expression, Antihypertensive Effect, and Underlying Mechanism of Sequence-Designed ACE Inhibitory Peptide YWLKP.
Q, L., N, S., C, Z., D, L., Z, L., & H, M. (2026). Heterologous Expression, Antihypertensive Effect, and Underlying Mechanism of Sequence-Designed ACE Inhibitory Peptide YWLKP.. Journal of agricultural and food chemistry. https://doi.org/10.1021/acs.jafc.6c08999
Q L, N S, C Z, D L, Z L, H M. Heterologous Expression, Antihypertensive Effect, and Underlying Mechanism of Sequence-Designed ACE Inhibitory Peptide YWLKP.. Journal of agricultural and food chemistry. 2026; doi: 10.1021/acs.jafc.6c08999
Q L, N S, C Z, et al. Heterologous Expression, Antihypertensive Effect, and Underlying Mechanism of Sequence-Designed ACE Inhibitory Peptide YWLKP.[J]. Journal of agricultural and food chemistry. 2026. DOI: 10.1021/acs.jafc.6c08999.
@article{q2026,
author = {Liang Q and Sun N and Zhu C and Li D and Liu Z and Mou H},
title = {Heterologous Expression, Antihypertensive Effect, and Underlying Mechanism of Sequence-Designed ACE Inhibitory Peptide YWLKP.},
journal = {Journal of agricultural and food chemistry},
year = {2026},
doi = {10.1021/acs.jafc.6c08999},
note = {PMID: 42584139},
}
TY - JOUR AU - Liang Q AU - Sun N AU - Zhu C AU - Li D AU - Liu Z AU - Mou H TI - Heterologous Expression, Antihypertensive Effect, and Underlying Mechanism of Sequence-Designed ACE Inhibitory Peptide YWLKP. T2 - Journal of agricultural and food chemistry PY - 2026 DO - 10.1021/acs.jafc.6c08999 AN - PMID:42584139 ER -
Rational sequence optimization is essential for transforming food-derived peptides into more potent angiotensin-converting enzyme (ACE) inhibitors. LYPVK and its sequence-designed derivative YWLKP exhibit potent activity; however, their binding mechanisms, transport routes, and in vivo antihypertensive effects remain unclear. Here, they were systematically investigated by biotechnological preparation, biolayer interferometry (BLI), molecular dynamics (MD) simulation, Caco-2 transport assays, and studies on spontaneously hypertensive rats (SHRs). BLI revealed that YWLKP bound to ACE with a subnanomolar affinity constant KD of (1.08 ± 0.40) × 10-9 M, consistent with MD results showing a more stable peptide-ACE complex. Caco-2 monolayer transport showed that LYPVK mainly permeated via the paracellular pathway, whereas YWLKP exhibited PepT1-mediated transport. In SHRs, both peptides significantly reduced blood pressure after single and long-term administration, accompanied by renin-angiotensin system modulation, reduced renal and cardiac impairment, and improved endothelial dysfunction. Collectively, these findings support YWLKP as a promising antihypertensive candidate for functional food applications.