Thiol-based angiotensin-converting enzyme 2 inhibitors: P1' modifications for the exploration of the S1' subsite.
Explorations of the S(1') subsite of ACE2 via modifications of the P(1') methylene biphenyl moiety of thiol-based metalloprotease inhibitors led to improvements in ACE2 selectivity versus ACE and NEP, while maintaining potent ACE2 inhibition.
Deaton
David N
DN
Department of Medicinal Chemistry, GlaxoSmithKline, Research Triangle Park, NC 27709, USA. david.n.deaton@gsk.com
Graham
Kevin P
KP
Gross
Jeffrey W
JW
Miller
Aaron B
AB
D000085962:Angiotensin-Converting Enzyme 2; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D001665:Binding Sites; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000737:chemistry* / Q000494:pharmacology*
D000806:Angiotensin-Converting Enzyme Inhibitors; D011994:Recombinant Proteins; D013438:Sulfhydryl Compounds; D007703:Peptidyl-Dipeptidase A; C000705307:ACE2 protein, human; D000085962:Angiotensin-Converting Enzyme 2