Covalent Binding of a Bucillamine Derivative with Albumin in Sera from Healthy Subjects and Patients with Various Diseases

  title={Covalent Binding of a Bucillamine Derivative with Albumin in Sera from Healthy Subjects and Patients with Various Diseases},
  author={Ryuichi Narazaki and Masaki Otagiri},
  journal={Pharmaceutical Research},
AbstractPurpose. To investigate the difference of pharmacokinetics of thiol-containing drugs in various disease states, we studied the covalent binding of SA3786, a bucillamine derivative, with proteins in patient serum compared with that in healthy serum. Methods. Sera from healthy volunteers and patients of various diseases were supplied by the Japanese Red Cross Kumamoto Hospital. For the formation of conjugate experiments, SA3786 was added to a final concentration of 7 × 10−4M. After 6h… 
A molecular functional study on the interactions of drugs with plasma proteins.
  • M. Otagiri
  • Biology, Chemistry
    Drug metabolism and pharmacokinetics
  • 2005
A topology analysis of drug binding sites on HSA and AGP was determined using various methods, including spectroscopy, QSAR, photoaffinity labeling and site directed mutagenesis, and Recombinant albumin was found to be useful for rapidly identifying drugbinding sites.
Practical aspects of the ligand-binding and enzymatic properties of human serum albumin.
A tabulation of high-affinity binding sites for both endogenous and exogenous compounds has been made; it could be useful for the above-mentioned purpose, but it could also be of value when trying to predict potential drug interactions at the protein-binding level.
Albumin in Medicine
Human serum albumin is synthesized in the liver and continuously secreted into the bloodstream, and it has enzymatic properties which are so pronounced that they most probably are of biological importance.
Albumin-drug interaction and its clinical implication.
Kinetic studies of covalent binding between N-acetyl-L-cysteine and human serum albumin through a mixed-disulfide using an N-methylpyridinium polymer-based column.
The binding properties of the disulfide covalent bond between N-acetyl-L-cysteine (NAC) and human serum albumin (HSA) were investigated to suggest that the interaction between NAC and HSA proceeds in a 2-step processes.
Cys34-Cysteinylated Human Serum Albumin Is a Sensitive Plasma Marker in Oxidative Stress-Related Chronic Diseases
In conclusion, ESI-TOFMS is a suitable high throughput method for the rapid and sensitive quantification of Cys-Cys34-HSA in a large number of samples for evaluating oxidative stress related chronic disease progression or in response to a treatment.
Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties
The physiological or pathophysiological concentrations of different oxidatively modified albumin molecules vary over a wide range and are crucial in assessing the clinical relevance of altered ligand binding properties of a particularly modifiedalbumin species in various disease conditions.
Human serum albumin: from bench to bedside.
Human Serum Albumin in Blood Detoxification Treatment
Molecular modification of the albumin domains through site-directed mutagenesis for strengthening toxin binding is a feasible approach for improving the efficiency and effectiveness of blood detoxification treatment.


Drug-protein conjugation and its immunological consequences.
The drug-Protein Conjugation and its Immunological Consequences have been studied in more detail in this review than in previous reviews of the subject.