81110-22-7Relevant articles and documents
Design, synthesis and evaluation of Fe-s targeted adenosine 5′-phosphosulfate reductase inhibitors
Paritala, Hanumantharao,Suzuki, Yuta,Carroll, Kate S.
, p. 199 - 220 (2015)
Adenosine 5′-phosphosulfate reductase (APR) is an iron-sulfur enzyme that is vital for survival of Mycobacterium tuberculosis during dormancy and is an attractive target for the treatment of latent tuberculosis (TB) infection. The 4Fe-4S cluster is coordinated to APR by sulfur atoms of four cysteine residues, is proximal to substrate, adenosine 5′-phopsphosulfate (APS), and is essential for catalytic activity. Herein, we present an approach for the development of a new class of APR inhibitors. As an initial step, we have employed an improved solid-phase chemistry method to prepare a series of N6-substituted adenosine analogues and their 5′-phosphates as well as adenosine 5′-phosphate diesters bearing different Fe and S binding groups, such as thiols or carboxylic and hydroxamic acid moieties. Evaluation of the resulting compounds indicates a clearly defined spacing requirement between the Fe-S targeting group and adenosine scaffold and that smaller Fe-S targeting groups are better tolerated. Molecular docking analysis suggests that the S atom of the most potent inhibitor may establish a favorable interaction with an S atom in the cluster. In summary, this study showcases an improved solid-phase method that expedites the preparation of adenosine and related 5′-phosphate derivatives and presents a unique Fe-S targeting strategy for the development of APR inhibitors.
HOMOLYTIC TRANSFORMATIONS OF 1,3-OXATHIOLANES IN THE PRESENCE OF POLYHALOMETHANES
Batyrbaev, N. A.,Zorin, V. V.,Zlotskii, S. S.,Rakhmankulov, D. L.
, p. 1160 - 1161 (2007/10/02)
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