A highly efficient method to synthesize diverse symmetrical phosphinic acids with the potential to act as pivotal candidates in the design of HIV-1 protease inhibitors has been developed. Such compounds have been designed based on the enzyme-substrate specificity, and their elongated analogues are expected to demonstrate significant inhibition against the HIV-1 protease with IC values in the low nanomolar range. Moreover, a highly efficient esterification protocol with carbohydrates and flavonoids has been devised to address the inherent absorption challenges associated with phosphinic-based drugs.
View Article and Find Full Text PDFNucleoside triphosphate diphosphohydrolases (NTPDases), an important class of ectonucleotidases, are responsible for the sequential hydrolysis of extracellular nucleotides. However, over-expression of NTPDases has been linked with various pathological diseases e.g.
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