1 research outputs found
Graphitized Porous Carbon for Rapid Screening of Angiotensin-Converting Enzyme Inhibitory Peptide GAMVVH from Silkworm Pupa Protein and Molecular Insight into Inhibition Mechanism
A novel hydrophobic hexapeptide with
high angiotensin-converting
enzyme (ACE) inhibitory activity was screened from silkworm pupa protein
(SPP) hydrolysate via graphitized porous carbon and reverse-phase
high-performance liquid chromatography methods. Graphitized porous
carbon derived from dopamine, possessing high surface area and high
graphitic carbon, was used to rapidly screen and enrich hydrophobic
peptides from SPP hydrolysate. The ACE inhibition pattern and mechanism
of the purified peptide were also systematically studied by the classic
Lineweaver–Burk model and by molecular docking/dynamic simulation.
The novel hydrophobic hexapeptide was identified as Gly-Ala-Met-Val-Val-His
(GAMVVH, IC<sub>50</sub> = 19.39 ± 0.21 μM) with good thermal/antidigestive
stabilities. Lineweaver–Burk plots revealed that GAMVVH behaved
as a competitive ACE inhibitor. It formed hydrogen bonds with S1 and
S2 pockets of ACE and established competitive coordination with ZnÂ(II)
of ACE. The synergy of hydrogen bonds with active pockets and ZnÂ(II)
coordination efficiently changed the three-dimensional structure of
ACE and thus inhibited bioactivity of ACE