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Bovine serum albumin potentiates caffeine- or ATP-induced tension in human skinned skeletal muscle fibers BJMBR
Human skinned muscle fibers were used to investigate the effects of bovine serum albumin (BSA) on the tension/pCa relationship and on the functional properties of the Ca2+-release channel of the sarcoplasmic reticulum (SR). In both fast- and slow-type fibers, identified by their tension response to pSr 5.0, BSA (0.7-15 µM) had no effect on the Ca2+ affinity of the contractile proteins and elicited no tension per se in Ca2+-loaded fibers. In contrast, BSA (>1.0 µM) potentiated the caffeine-induced tension in Ca2+-loaded fibers, this effect being more intense in slow-type fibers. Thus, BSA reduced the threshold caffeine concentration required for eliciting detectable tension, and increased the amplitude, the rate of rise and the area under the curve...
Palavras-chave: Calcium-release channel; Sarcoplasmic reticulum; Human muscle fiber; Bovine serum albumin; Caffeine.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000500017
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Bovine serum albumin-based nanoparticles containing the flavonoid rutin produced by nano spray drying BJPS
Pedrozo,Regiellen Cristina; Antônio,Emilli; Khalil,Najeh Maissar; Mainardes,Rubiana Mara.
Rutin is a flavonoid compound obtained from different vegetables and fruits; specifically, it is found in the seeds of buckwheat and in fruit peels, particularly citrus. It is also an important constituent of red wine. Rutin exhibits various biological properties including antiviral, vasoprotective, anti-inflammatory, and anticarcinogenic activities. However, its antioxidant activity is the most well studied. Despite the potential for in vitro applications, rutin presents low oral bioavailability that affects its biological activities. Nanoparticles composed of polymers, protein, or lipids are of great importance in the pharmaceutical and nutraceutical areas due to their physicochemical properties, which improve the pharmacokinetics of the drug which is...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Nano spray drying; Rutin; Nanoparticles; Bovine serum albumin; Antioxidant.
Ano: 2020 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-82502020000100512
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Photophysical studies of zinc phthalocyanine and chloroaluminum phthalocyanine incorporated into liposomes in the presence of additives BJMBR
Nunes,S.M.T.; Sguilla,F.S.; Tedesco,A.C..
The photophysical properties of zinc phthalocyanine (ZnPC) and chloroaluminum phthalocyanine (AlPHCl) incorporated into liposomes of dimyristoyl phosphatidylcholine in the presence and absence of additives such as cholesterol or cardiolipin were studied by time-resolved fluorescence, laser flash photolysis and steady-state techniques. The absorbance of the drugs changed linearly with drug concentration, at least up to 5.0 µM in homogeneous and heterogeneous media, indicating that aggregation did not occur in these media within this concentration range. The incorporation of the drugs into liposomes increases the dimerization constant by one order of magnitude (for ZnPC, 3.6 x 10(4) to 1.0 x 10(5) M-1 and for AlPHCl, 3.7 x 10(4) to 1.5 x 10(5) M-1), but this...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Zinc phthalocyanine; Chloroaluminum phthalocyanine; Bovine serum albumin; Liposomes; Cholesterol; Cardiolipin; Dimyristoyl phosphatidylcholine.
Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000200016
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Spectroscopic studies on the interaction of efonidipine with bovine serum albumin BJMBR
Wang,N.; Ye,L.; Zhao,B.Q.; Yu,J.X..
Efonidipine hydrochloride is an antihypertensive and antianginal agent with fewer side effects and is better tolerated in the treatment of hypertension with renal impairment. Its interaction with bovine serum albumin (BSA) is of great use for the understanding of the pharmacokinetic and pharmacodynamic mechanisms of the drug. The binding of efonidipine to BSA was investigated by fluorescence spectroscopy and circular dichroism. BSA fluorescence was quenched by efonidipine, due to the fact that efonidipine quenched the fluorescence of tryptophan residues mainly by the collision mode. The thermodynamic parameters ΔH0 and ΔS0 were 68.04 kJ/mol and 319.42 J·mol-1·K-1, respectively, indicating that the hydrophobic interactions played a major role. The results...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Efonidipine; Bovine serum albumin; Fluorescence quenching; Synchronous fluorescence; Circular dichroism.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000700007
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