Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I

When a drug interacts with its receptor, the nonpolar substituent of and receptor proteins attract each other because they have opposite magnitude respect to other. X-rays structure studies reflected that S2/S2’ pocket in HIV-1 protease enzyme are essentially hydrophobic. The residues make up these pockets Val-32, Ile-47, Ile-50, Ile-84 monomeric polypeptidic unit enzyme. Δπdr ΔSASAdr been used measure extent hydrophobic interaction between peptidic inhibitors (binding site: valine‒isoleucine; catalytic glycine‒aspartic acid‒threonine) on For measurement interaction, molecular modeling geometry optimization all amino acids carried out CAChe Pro software by opting semiempirical PM3 methods. Log P was calculated using atom-typing scheme Ghose Crippen, while solvent accessible surface area conductor likes screening model. πd, πr, SASASd SASASr well describe hydrophobicities substituents play effective role for site selectivity receptor. Comparative study values show order acids: Asp > Thr Val Ile Ile, respectively. Further, comparative (ΣΔπdr)binding-site, (ΣΔπdr)catalytic-site, (ΣΔSASAdr)binding-site, (ΣΔSASAdr)catalytic-site shows HIV-1-PRIs interact binding rather than as lower value ΣΔπdr ΣΔSASAdr. Among site, has maximum it vale ΔSASAdr.