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• W3040390118 endingPage "8579" @default.
• W3040390118 startingPage "8570" @default.
• W3040390118 abstract "Herein we report the interaction of 3-hydroxyflavone (3HF) with various isomeric forms of Human Serum Albumin (HSA), namely, the N-isoform (or native HSA at pH 7.4) and the B-isoform (at pH 9.2). Spectroscopic signatures of 3HF reveal that the interaction of 3HF with the N-isoform of HSA results in significant lowering of absorbance of the neutral species (λabs ∼ 345 nm) with concomitant increase of the anionic species (λabs ∼ 416 nm) whereas interaction with the B-isoform of HSA leads to selective enhancement of absorbance of the anionic species. The fluorescence profile of 3HF displays marked increase of intensity of the proton transferred tautomer (λem ∼ 538 nm) as well as the anionic species (λem ∼ 501 nm) for both the forms of the protein. However, analyses of the associated thermodynamics through temperature-dependent isothermal titration calorimetric (ITC) indicate that the interaction of 3HF with the N-isoform of HSA is more enthalpic in the lower temperature limit while the entropy contribution predominates in the higher temperature limit. Consequently, the 3HF–HSA (N-isoform at pH 7.4) interaction reveals an unusual thermodynamic signature of a positive heat capacity change (ΔCp = 3.84 kJ mol–1K–1) suggesting the instrumental role of hydrophobic hydration. On the contrary, the 3HF–HSA (B-isoform at pH 9.2) interaction shows qualitatively reverse effect. Consequently, the interaction is found to be characterized by an enthalpy-dominated hydrophobic effect (negative heat capacity change, ΔCp = −1.15 kJ mol–1K–1) which is rationalized on the basis of the nonclassical hydrophobic effect." @default.
• W3040390118 created "2020-07-10" @default.
• W3040390118 creator A5003037418 @default.
• W3040390118 creator A5043280233 @default.
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• W3040390118 creator A5052565373 @default.
• W3040390118 creator A5076398641 @default.
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• W3040390118 date "2020-06-29" @default.
• W3040390118 modified "2023-10-11" @default.
• W3040390118 title "Contrasting Thermodynamics Governs the Interaction of 3-Hydroxyflavone with the N-Isoform and B-Isoform of Human Serum Albumin" @default.
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• W3040390118 doi "https://doi.org/10.1021/acs.langmuir.0c01362" @default.
• W3040390118 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32600049" @default.
• W3040390118 hasPublicationYear "2020" @default.
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