HIV-1 Protease Inhibitory Activity of Lectin Obtained from Soybean (Glycine max), Betel Nut Palm Seed (Areca catechu), and Mung Bean Sprout (Vigna RADIATA)

Abstract

HIV attacks the immune system and relies on HIV-1 protease, an aspartyl protease essential for processing viral polyproteins and replication, making the enzyme a target for antiretroviral therapy. Natural lectins, known for antiviral properties, are being explored as potential inhibitors of HIV-1 protease. This study evaluated the inhibitory effects of lectins extracted from Soybean (Glycine max), Betel-Nut Palm Seed (Areca catechu), and Mung Bean Sprout (Vigna radiata) against HIV-1 protease. A true experimental design was used to determine each lectin’s percent inhibition and IC₅₀ value. Soybean lectin exhibited the most consistent dose-dependent inhibition, reaching 47.76% at 1000 μg/mL with an IC₅₀ of 499.88 μg/mL and moderate variability (SD = 36.93), suggesting a strong interaction with the enzyme. Betel nut lectin showed minimal inhibition at low concentrations, but reached 55.05% at 1000 μg/mL, the highest of the three, though with a higher IC₅₀ (689.61 μg/mL), indicating lower potency. Mung bean lectin showed inconsistent activity at low doses, peaking at 60.21% at 750 μg/mL before slightly declining, with an IC₅₀ of 524.79 μg/mL and the lowest standard deviation. Overall, Soybean lectin showed the most consistent inhibition, while Mung bean and Betel nut lectins demonstrated potential at higher concentrations.