The ability of 8-methoxypsoralen (8-MOP) to bind human serum albumin has been investigated in vitro through equilibrium dialysis and fluorescence quenching. By means of the first technique it was observed that, at concentrations presumably close to those obtainable in vivo following its administration in the photochemotherapy of psoriasis, over 80% of 8-MOP was bound to serum albumin. In human serum albumin fluorescence techniques revealed a preferential site of binding for 8-MOP with a high binding constant (Ka = 0.7 x 105 M-1) and precise steric requirements, since small conformational variations of the protein molecule were able to abolish its affinity for furocoumarin.
The binding of 8-methoxypsoralen by human serum albumin.
SCHIAVON, ODDONE;
1978
Abstract
The ability of 8-methoxypsoralen (8-MOP) to bind human serum albumin has been investigated in vitro through equilibrium dialysis and fluorescence quenching. By means of the first technique it was observed that, at concentrations presumably close to those obtainable in vivo following its administration in the photochemotherapy of psoriasis, over 80% of 8-MOP was bound to serum albumin. In human serum albumin fluorescence techniques revealed a preferential site of binding for 8-MOP with a high binding constant (Ka = 0.7 x 105 M-1) and precise steric requirements, since small conformational variations of the protein molecule were able to abolish its affinity for furocoumarin.
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