Minimum Structural Requirements for Minoxidil Inhibition of Lysyl Hydroxylase in Cultured Fibroblasts

    Sohail Murad, Lon C. Walker, Setsuko Tajima, Sheldon R. Pinnell
    Image of study
    TLDR Minoxidil needs specific structure to block lysyl hydroxylase; exploring alternatives may keep benefits without this effect.
    The study investigated the structural requirements for minoxidil inhibition of lysyl hydroxylase in cultured fibroblasts. Minoxidil was found to selectively inhibit lysyl hydroxylase, and several structural analogs of minoxidil were tested for their inhibitory potential. The results showed that minoxidil analogs with modified pyrimidine or piperidine ring decreased the level of lysyl hydroxylase activity, and a structural analog of minoxidil in which the piperidine ring had been replaced with an N,N-diethyl group was also found to suppress lysyl hydroxylase activity. The study concluded that an organic moiety containing a tertiary nitrogen para to the nitroxide oxygen is required for minoxidil inhibition of lysyl hydroxylase. The study suggests exploring minoxidil analogs that retain antihypertensive activity or ability to stimulate hair growth but lose the ability to suppress lysyl hydroxylase activity.
    View this study on →