Interaction of albumins from different species with phospholipid liposomes. Multiple binding sites system

Dimitrova, Mariana N.; Matsumura, Hideo; Dimitrova, A.; Neitchev, V.

doi:10.1016/s0141-8130(00)00123-9

Cited by 40 publications

(24 citation statements)

References 24 publications

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“…Careful control experiments are needed to compensate for bulk effects such as the heat of dilution of the ligand and the receptor, and the heat of mixing [102,103]. ITC has been routinely used to study many types of binding reactions [101,103,104,105,106] including, protein-protein [107], protein-membrane [108,109,110,111], and drug-receptor [106,112] interactions.…”

Section: Calorimetrymentioning

confidence: 99%

Label-free screening of bio-molecular interactions

Cooper

2003

Analytical and Bioanalytical Chemistry

415

297

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The majority of techniques currently employed to interrogate a biomolecular interaction require some type of radio- or enzymatic- or fluorescent-labelling to report the binding event. However, there is an increasing awareness of novel techniques that do not require labelling of the ligand or the receptor, and that allow virtually any complex to be screened with minimal assay development. This review focuses on three major label-free screening platforms: surface plasmon resonance biosensors, acoustic biosensors, and calorimetric biosensors. Scientists in both academia and industry are using biosensors in areas that encompass almost all areas drug discovery, diagnostics, and the life sciences. The capabilities and advantages of each technique are compared and key applications involving small molecules, proteins, oligonucleotides, bacteriophage, viruses, bacteria, and cells are reviewed. The role of the interface between the biosensor surface (in the case of SPR and acoustic biosensors) and the chemical or biological systems to be studied is also covered with attention to the covalent and non-covalent coupling chemistries commonly employed.

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Section: Calorimetrymentioning

confidence: 99%

Label-free screening of bio-molecular interactions

Cooper

2003

Analytical and Bioanalytical Chemistry

415

297

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“…Calorimetric titration studies indicated the binding of empty liposomes to the albumin species. The albumin molecules from different species adsorb strongly to phosphatidylcholine liposomes due mainly to the action of hydrophobic dehydration forces and entropy gain (39). In this way, the liposomes themselves increase the K b to BSA.…”

Section: Interaction Of Znpc and Alphcl With Bovine Serum Albumin In mentioning

confidence: 99%

Photophysical studies of zinc phthalocyanine and chloroaluminum phthalocyanine incorporated into liposomes in the presence of additives

Nunes

Sguilla

Tedesco

2004

Braz J Med Biol Res

177

100

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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 timeresolved 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 magni-

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“…From the titration, a complete binding isotherm is obtained as a plot of the heat change versus the molar ratio of protein to lipid. Thus far, the ITC assay has been used for several peripheral proteins, including apolipoprotein A-I (61), a major heparin-binding protein PDC-109 (62), P-glycoprotein (63), and serum albumin (64). The main advantage of the ITC assay is its accuracy since the binding is measured under true equilibrium conditions without sample modification and immobilization.…”

Section: Calorimetric Assaysmentioning

confidence: 99%