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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.0c01362
|2 doi
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|a pubmed24n1039.xml
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|a (DE-627)NLM311781225
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|a (NLM)32600049
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|a DE-627
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|e rakwb
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|a eng
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|a Nandy, Atanu
|e verfasserin
|4 aut
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|a Contrasting Thermodynamics Governs the Interaction of 3-Hydroxyflavone with the N-Isoform and B-Isoform of Human Serum Albumin
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|c 2020
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|a Text
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|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 21.06.2021
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|a Date Revised 21.06.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Flavonoids
|2 NLM
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|a Protein Isoforms
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|a Serum Albumin, Human
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|a ZIF514RVZR
|2 NLM
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|a 3-hydroxyflavone
|2 NLM
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|a ZTG9LSS5QH
|2 NLM
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|a Pramanik, Ushasi
|e verfasserin
|4 aut
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|a Mahato, Paritosh
|e verfasserin
|4 aut
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|a Shekhar, Shashi
|e verfasserin
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|a Paul, Bijan K
|e verfasserin
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|a Mukherjee, Saptarshi
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 36(2020), 29 vom: 28. Juli, Seite 8570-8579
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:36
|g year:2020
|g number:29
|g day:28
|g month:07
|g pages:8570-8579
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|u http://dx.doi.org/10.1021/acs.langmuir.0c01362
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