Table 2.
Hydrolysis of ACE2-substrate peptides by B38-CAP.
| Substrate | ACE2* | B38-CAP | Sequence |
|---|---|---|---|
| Angiotensin I | + | + | DRVYIHPFH↓L |
| Angiotensin 1–9 | − | + | DRVYIHPF↓H |
| Angiotensin II | + | + | DRVYIHP↓F |
| Angiotensin 1–7 | − | − | DRVYIHP |
| Apelin-13 | + | + | QRPRLSHKGPMP↓F |
| Apelin-36 | + | + | …QRPRLSHKGPMP↓F |
| des-Arg9-bradykinin | + | + | RPPGFSP↓F |
| Lys-des-Arg9-bradykinin | + | + | KRPPGFSP↓F |
| β-Casomorphin | + | + | YPFVEP↓I |
| Dynorphin A 1–13 | + | + | YGGFLRRIRPKL↓K |
| Ghrelin | + | + | …ESKKPPAKLQP↓R |
| Neurotensin 1–8 | + | + | pE-LYENKP↓R |
Summary of cleavability of peptides by B38-CAP. “+” indicates that it is cleaved with ACE2 or B38-CAP, whereas “−” means it is not cleaved. HPLC analyses for the metabolites of each peptide after B38-CAP treatment are shown in Supplementary Fig. 4a. *Cleavability of the peptides by ACE2 is from ref. 6.