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Serum protein-binding characteristics of vancomycin
H Sun1, E G Maderazo, A R Krusell
1Medical Research Laboratory, Hartford Hospital, Connecticut 06115.
Antimicrobial Agents and Chemotherapy
|May 1, 1993
Summary
Vancomycin primarily binds to albumin and immunoglobulin A (IgA) in serum. High IgA levels, seen in IgA myeloma, may lead to ineffective vancomycin treatment despite high total drug concentrations.
Area of Science:
- Pharmacology
- Immunology
- Clinical Chemistry
Background:
- Vancomycin serum protein binding is complex.
- Abnormal binding has been reported with high immunoglobulin A (IgA) levels.
Purpose of the Study:
- To investigate vancomycin binding characteristics to specific serum proteins.
- To elucidate the mechanism behind altered vancomycin binding at high IgA concentrations.
Main Methods:
- Ultrafiltration for separating free and bound vancomycin.
- High-performance liquid chromatography (HPLC) for drug concentration measurement.
- Studied binding to alpha-1 acid glycoprotein, IgG, IgM, IgA, and albumin.
Main Results:
- Vancomycin does not bind to alpha-1 acid glycoprotein, IgG, or IgM.
- Major binding occurs with albumin and IgA, fully explaining total binding.
- Vancomycin preferentially binds to IgA (NK = 4.3 x 10^5 M^-1) over albumin (NK = 527.5 M^-1).
Conclusions:
- Vancomycin binding is primarily to albumin and IgA.
- Elevated IgA levels can lead to high total vancomycin concentrations.
- This may paradoxically result in clinically ineffective vancomycin therapy.