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High levels of GLO-I have also been associated with multidrug resistance, metastasis, and poor clinical outcomes,11,12 highlighting its potential as a therapeutic target for anticancer drug development.12,13 Structurally, GLO-I is a homodimeric, zinc-dependent metalloenzyme consisting of two identical polypeptide chains of 183 amino acid residues each (Figure 2A and B).12,14 The dimer interface houses the catalytically active site and is characterized by three binding sites: a deep hydrophobic pocket, a central zinc (Zn 2+ ) ion, and a positively charged entrance (Figure 2C).12,14 The entrance is delineated by Arg37, Arg122, Lys150, and Lys156 residues, while the Zn 2+ ion is collectively stabilized by coordination with Gln33, Glu99, His126, and Glu172.12,14 Through the years, several strategies in drug discovery have been adopted to identify inhibitors of GLO-I
