1 research outputs found
High-Throughput and Rapid Screening of Novel ACE Inhibitory Peptides from Sericin Source and Inhibition Mechanism by Using in Silico and in Vitro Prescriptions
Several
novel peptides with high ACE-I inhibitory activity were
successfully screened from sericin hydrolysate (SH) by coupling in
silico and in vitro approaches for the first time. Most screening
processes for ACE-I inhibitory peptides were achieved through high-throughput
in silico simulation followed by in vitro verification. QSAR model
based predicted results indicated that the ACE-I inhibitory activity
of these SH peptides and six chosen peptides exhibited moderate high
ACE-I inhibitory activities (log IC<sub>50</sub> values: 1.63–2.34).
Moreover, two tripeptides among the chosen six peptides were selected
for ACE-I inhibition mechanism analysis which based on Lineweaver–Burk
plots indicated that they behave as competitive ACE-I inhibitors. The C-terminal residues
of short-chain peptides that contain more H-bond acceptor groups could
easily form hydrogen bonds with ACE-I and have higher ACE-I inhibitory
activity. Overall, sericin protein as a strong ACE-I inhibition source
could be deemed a promising agent for antihypertension applications