A High Performance Theory for Thermodynamic Study on the Binding of Human Serum Albumin with Erbium Chloride

Behbehani, G. Rezaei; Divsalar, Adeleh; Saboury, Ali Akbar; Faridbod, Farnoush

doi:10.1002/cjoc.200990046

Cited by 6 publications

(1 citation statement)

References 36 publications

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“…In 2009 we identified more than 400 articles after searching Web of Science, PubMed, SciDir and OVID databases using ‘isothermal AND titration AND calorimetry’ or ITC or ‘Isothermal Titration Calorimetry’ search terms. These have been classified into the following categories: Pre‐2009 references cited in the text and review articles 1–43 Protein‐protein and protein‐peptide interactions 44–124 Protein/peptide‐small molecule interactions 125–218 Protein/peptide‐metal ion interactions 219–253 Protein/peptide‐nucleic acid interactions 254–273 Protein/peptide‐lipid interactions 274–292 Protein/peptide‐polysaccharide interactions 293–316 Nucleic acid‐small molecule interactions 317–348 Small molecule interactions …”

Section: Introductionmentioning

confidence: 99%

Survey of the year 2009: applications of isothermal titration calorimetry

Falconer

Collins

2010

J. Mol. Recognit.

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Isothermal titration calorimetry (ITC) is now an established and invaluable method for determining the thermodynamic constants, association constant and stoichiometry of molecular interactions in aqueous solutions. The technique has become widely used by biochemists to study protein interaction with other proteins, small molecules, metal ions, lipids, nucleic acids and carbohydrates; and nucleic acid interaction with small molecules. The drug discovery industry has utilized this approach to measure protein (or nucleic acid) interaction with drug candidates. ITC has been used to screen candidates, guide the design of potential drugs and validate the modelling used in structure-based drug design. Emerging disciplines including nanotechnology and drug delivery could benefit greatly from ITC in enhancing their understanding and control of nano-particle assembly, and drug binding and controlled release.

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Section: Introductionmentioning

confidence: 99%

Survey of the year 2009: applications of isothermal titration calorimetry

Falconer

Collins

2010

J. Mol. Recognit.

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A Thermodynamic Study on the Binding of Human Serum Albumin with Lanthanum Ion

et al. 2010

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Thermodynamics of the interaction between lanthanum(III) ion, La 3＋ , and human serum albumin (HSA), was investigated at pH 7.0 and 300 K in Tris-HCl buffer by isothermal titration calorimetry. A solvation model was used to reproduce the enthalpies of HSA interaction with La 3＋ . The solvation parameters recovered from our new model were attributed to the structural change of HSA and its biological activity. The interaction of HSA with La 3＋showed a set of two binding sites with negative cooperativity.

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