The theoretical investigation of the binding mode between human serum albumin and penicillins

Aim To investigate theoretically the binding mode between human serum albumin and penicillins. Methods Molecular docking method was used to elucidate the binding modes between human serum albumin (HSA) and penicillins. Results The lowest binding energies (LBE) of apalcillin, oxacillin, carbenicillin, ampicillin, amoxicillin were 44.2, 46.5, 42.1, 40.9, 40.7 kcal/mol,respectively. Subdomain IIA and IB are more easy to bind with penecillins than others. Conclusion Penicillins may be easy to bind to the cavity IIA and IB. Molecules with both polar and nonpolar two parts may be easy to bind to the cavities of HSA.