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 IC50 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. These esters not only exhibit low toxicity but also have the potential to generate flavonoid moieties in situ, which are associated with hepatoprotective effects, or naturally occurring carbohydrate metabolites. The methodology utilizes effective peptide coupling reagents, such as aminium-based TBTU and carbodiimide-based DIC, and affords the target products in excellent to quantitative yields. This research represents a promising avenue for the development of novel HIV-1 protease inhibitors with significant therapeutic benefits.
© 2024 The Authors. Published by American Chemical Society.