Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isolation of acidic and basic model drugs by using pH sensitive poly(acrylic acid) grafted poly(vinylidene fluoride) (PAA-PVDF) cation-exchange membrane from biological fluids was reported. Effects of drug charge and lipophilicity on adsorption were also investigated. In the present study, basic model drugs adsorbed to a considerably greater extent onto the membrane than acidic drugs. Albumin was not adsorbed onto the membrane. Results of our study exposed, that electrostatic interactions between positively charged basic drug and negatively charged PVDF-PAA membrane were the most important factor affecting drug adsorption onto the membrane. Adsorption of acidic and basic drugs onto the PVDF-PAA membrane was not related to drug lipophilicity. The results of present study demonstrated that basic drugs adsorbed extensively onto the membrane, but albumin did not, proposing that PAA-PVDF membrane may be suitable for isolating basic drugs from proteinaceous biological fluids (i.e. serum) for subsequent monitoring and evaluation.
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PMID:Isolation of drugs from biological fluids by using pH sensitive poly(acrylic acid) grafted poly(vinylidene fluoride) polymer membrane in vitro. 1747 55

The complex formation of Bovine Serum Albumin (BSA) with anionic polyelectrolyte (polyacrylic acid, PAA) in aqueous solution was studied by a fluorescence technique, pH titration and HPLC analysis. The character of the interactions and solubility of the polycomplex particles depends on the BSA/PAA ratios and the pH of solution. The interaction at pH > pI (isoelectric point of BSA) (pH 6.0-7.0) is negligible weak and at pH 5.0 results with the formation of stable water-soluble polycomplexes at a wide range of protein/polymer ratios. The fluorescence intensity of BSA sharply decreased when an different amount of PAA was added and its maximum wavelength shifts towards the blue region. The protein molecules in the structure of soluble polycomplex particles are densely covered by the shelf of a polymer coil and practically "fenced off" from the water environment. This effect was reinforced by the increase of protein components. Existence of soluble and insoluble PAA-BSA complexes have been observed at pH < pI (pH 4.0-4.3). These soluble complexes characterized by the structure of particles in which protein molecules are densely covered by the shelf of a polymer coil. By the increase in the protein concentration, these complexes aggregate to an interpolymer species.
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PMID:The Fluorescence Study of Interaction Between Bovine Serum Albumin and Polyacrylic Acid. 1939 96

Complex coacervation can be used as a route to compartmentalize a variety of solutes such as organic small molecules, inorganic nanoparticles, and proteins within microscale coacervate droplets. To obtain insight into the accumulation of proteins within complex coacervate phases, the encapsulation of Bovine Serum Albumin (BSA) within complex coacervates containing cationic polyelectrolyte poly(allylamine hydrochloride) (PAH) and anionic polyelectrolyte poly(acrylic aid) (PAA) was investigated as a function of mixing sequence, total polyelectrolyte concentration, BSA overall concentration, and the mixing molar ratio of PAA/PAH. Mixing BSA having a negative net charge with the polycation PAH before coacervation, increasing the total polyelectrolyte concentration and PAA/PAH molar ratio, or decreasing the BSA overall concentration led to more efficient protein encapsulation. Preservation of the secondary structure of BSA during the complex coacervation process was confirmed using circular dichroism spectroscopy. Our study shows that PAA-PAH coacervates can serve as a protective system against the denaturation of BSA when exposed to extremes of pH, high temperatures, as well as in solution of urea. Additionally, it was found that by encapsulation of proteins within coacervates via complex coacervation, the complexation between proteins and heavy metal can be efficiently inhibited. Protection of BSA against severe environmental conditions via encapsulation within polyelectrolyte coacervates provides new insights and methods to issues of maintaining stability and function of proteins.
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PMID:Protein encapsulation via polyelectrolyte complex coacervation: Protection against protein denaturation. 3038 71