IndraLab

Statements


Pro-Phe inhibits ACE2. 5 / 5
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"The active site model was able to help design new ACE2 inhibitors, for example the presence of Pro Phe in the concentration of 180 microM could inhibit ACE2 activity (Guy et al., 2003b)."

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"A broad range of ACE inhibitors, such as captopril and lisinopril does not affect the activity of ACE2, whereas ACE2 activity is inhibited by the dipeptide Pro Phe, and specific ACE2 inhibitors, such as the peptide analogues DX600 and MLN 4760 ((S, S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoicacid) have been developed."

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"The dipeptide, Pro Phe, completely inhibits ACE2 activity at 180 microM with angiotensin II as the substrate."

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"XREF_BIBR, XREF_BIBR This cleavage preference of ACE2 was supported by a key experiment in which a dipeptide, Pro Phe, completely inhibited ACE2 activity at 180 muM with Ang II as the substrate."

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"The active site model was able to help design new ACE2 inhibitors, for example the presence of Pro Phe in the concentration of 180muM could inhibit ACE2 activity."