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Molecular insights into trypanothione reductase‐inhibitor interaction: A structure‐based review
Author(s) -
Tiwari Neha,
Tanwar Neetu,
Munde Manoj
Publication year - 2018
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.201700373
Subject(s) - drug discovery , computational biology , protein data bank , mechanism (biology) , antiparasitic , chemistry , drug , protein data bank (rcsb pdb) , antiparasitic agent , pharmacology , protein structure , biochemistry , biology , medicine , philosophy , epistemology , pathology
Information on how small molecules bind to the target enzyme has the potential to impact immensely on how medicinal chemists go about antiparasitic drug discovery. In this review, for the first time, we intend to make an assessment of the structural aspects of trypanothione reductase as drug target, and its complexes with several reversible drugs from the Protein Data Bank (PDB). We attempt to reveal the mechanism of these interactions by careful accounting of the X‐ray structures and their possible roles in biological activity to treat Trypanosomatidae diseases. We focus on some of the outstanding findings from structures that are relevant to anti‐trypanocidal drug discovery. We also review new interesting compounds that have appeared in the literature based on these X‐ray structures.