作者： Carlo Bertucci , Maria Chiara Barsotti , Andrea Raffaelli , Piero Salvadori
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摘要: Covalent and reversible binding of penicillins to human serum albumin (HSA) are known to occur in physiological conditions [1]. The appearance of modified forms of the protein has been observed in patients taking high dosages of the antibiotics. The reaction involves penicillin β-lactam ring and ε-aminogroups of several lysines. The penicillin-HSA conjugate represents the main antigenic determinant for phenomena of allergy to the antibiotic [2]. In this study the reaction of penicillin G with recombinant human albumin (rHA) has been investigated in vitro, in function of time of incubation and antibiotic concentration. The concentrations of the drug were chosen as representative of clinical dosages. Mass spectrometry has been used for evaluating the extent of modification. This methodology allowed to reveal the presence of covalently bound penicillin only for high [antibiotic]/[albumin] ratios. The number of bound …