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Human NOS isozymes were also inhibited by 7, which lacks an amino group on the pyridine moiety.
The 2-aminopyridine-containing l-amino acids 8 had potent inhibitory activity toward all of the human NOS isozymes.
All 3 human NOS isoforms, nNOS, eNOS (endothelial NOS), and iNOS (inducible NOS) have nearly identical active site structures thus making selective inhibitor design especially difficult.
S-Methyl l-thiocitrulline (Furfine et al., 1994) is also used, albeit less frequently, to selectively inhibit nNOS in vitro and in vivo, yet studies show that the compound is <10-fold selective for isolated nNOS over eNOS (Furfine et al., 1994; Boer et al., 2000; both using human NOS isozymes).
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