No abstract

22The study focuses on identification of ACE-inhibitory peptides from the proteolytic digests of muscle 23 protein of Bellamya bengalensis and its underlying mechanism. 120 min Alcalase-hydrolysates were 24 ultrafiltered to isolate the small peptide fraction (<3kDa) and in vitro ACE-inhibitory activity was 25 analyzed. The IC 50 value of the 120 min hydrolysate ultafiltered fraction was found to be 86.74 ± 0.575 26 µg/mL, while the IC 50 of Lisinopril is 0.31 ± 0.07 µg/mL. This fraction was assessed in MALDI-ToF 27 mass-spectrometer and five peptides were sequenced via de novo sequencing. The ACE-inhibitory 28 potential of the peptides have a positive correlation with the hydrophobicity of the amino acids. 29 Synthetic analogue of the peptide (IC 50 value 8.52 ± 0.779 µg/mL) was used to understand the 30 thermodynamics of the inhibition by checking the binding affinity of the peptide to ACE by Isothermal 31 titration calorimetry compared with lisinopril, and further substantiated by in silico site specific 32 molecular docking study.33 34