First-derivative spectroscopic determination of binding characteristics of rifampicin to human albumin and serum.
A first-derivative spectroscopic method for the simultaneous determination of bound and unbound drug in human serum and serum albumin solution was developed. As an example, the binding characteristics of rifampicin were studied. In serum albumin solution, the rifampicin bound and unbound fractions were determined at 473.5 and 475.8 nm, respectively. For human serum, the unbound fraction was determined at 479.4 nm. The results obtained by the first-derivative spectroscopic method were in agreement with those obtained by equilibrium dialysis. The proposed method is very simple and accurate when applied to measurements of drug:protein binding. Moreover, it allows a direct measurement of the bound and unbound forms without any physical separation.
Lachau
S
S
Laboratoire de Pharmacocinétique, Faculté des Sciences Pharmaceutiques, Toulouse, France.
Rochas
M A
MA
Tufenkji
A E
AE
Martin
N
N
Levillain
P
P
Houin
G
G
D006801:Humans; D011485:Protein Binding; D012293:Rifampin / Q000097:blood*; D012709:Serum Albumin / Q000378:metabolism*; D013053:Spectrophotometry / Q000379:methods; D013057:Spectrum Analysis / Q000379:methods
D012709:Serum Albumin; D012293:Rifampin