A synthetic pathway to Cys-Xxx-Cys (N2S2) analogue ligands: An improved synthesis of HSCH2CH2C(O)NHCH 2C(O)NHCH2CH2SH
Herein, two improved synthetic pathways to biologically relevant Cys-Xxx-Cys analogue ligands used in conjunction with metals as metalloenzyme models (Ni for carbon monoxide dehydrogenase/acetyl-CoA synthase A-cluster; Co and Fe for nitrile hydratase) are reported. Copyright Taylor & Francis Group, LLC.
Angelosante, Jennifer K.,Lewis, Breia J.,Cooper, Lisa E.,Swanson, Rebecca A.,Daley, Christopher J. A.
p. 2263 - 2272
(2007/10/03)
Metal-chelating inhibitors of a zinc finger protein HIV-EP1. Remarkable potentiation of inhibitory activity by introduction of SH groups
HIV-EP1 is a C2H2 type zinc finger protein which binds to DNA κB site present in the long terminal repeat of HIV provirus. Previously we have reported zinc chelators having histidine-pyridine-histidine skeleton and were successful in inhibiting the DNA binding of HIV-EP1 by removing zinc from the zinc finger domain. Aiming at the potentiation of the inhibitory activity of our previous zinc chelators, herein synthesized were novel chelators comprising pyridine and aminoalkanethiol. These showed marked inhibitory activity on the DNA binding of HIV-EP1. In particular, one of them having a bis(2-mercaptoethyl)amino side chain showed inhibitory activity (IC50, ~4 μM) 10 times stronger than that of the strongest inhibitor that we reported previously. It appeared that these inhibited the DNA binding of HIV-EP1 by a mechanism distinct from that of the previous histidine-based inhibitors.
Fujita, Mikako,Otsuka, Masami,Sugiura, Yukio
p. 503 - 507
(2007/10/03)
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