Table 4.
Structural characteristics and inhibition of ACE inhibitory peptides from mushrooms.
| ACE Inhibitory Peptide Sequence | Amino Acid Residues | pI | GRAVY * | IC50 (µM) | Mode of Inhibition |
|---|---|---|---|---|---|
| RIGLF | 5 | 9.75 | 1.240 | 116 | Competitive |
| AHEPVK | 6 | 6.79 | −1.033 | 63 | Competitive |
| PSSNK | 5 | 9.18 | −2.120 | 129 | Non-competitive |
| VIEKYP | 6 | 5.97 | −0.267 | 130 | Competitive |
| LSMGSASLSP | 10 | 5.52 | 0.61 | 335 | Non-competitive |
| GQP | 3 | 5.52 | n.d. | 3.2 | Competitive |
| GQGGP | 5 | 5.52 | −1.260 | 254 | Competitive |
| RLPSEFDLSAFLRA | 14 | 6.07 | 0.100 | 52 | Competitive |
| RLSGQTIEVTSEYLFRH | 17 | 6.76 | −0.488 | 1079 | Non-competitive |
* The grand average of hydropathicity (GRAVY) value was obtained by analyzing the peptide amino acid residues with ProtParam tool via Expasy; n.d., not determined since at least 5 amino acid residues are required for the analysis; pI, isoelectric point.