An interaction of the functionalized closo -borates with albumins: The protein fluorescence quenching and calorimetry study

Losytskyy, Mykhaylo Yu.; Kovalska, Vladyslava; Varzatskii, Оleg А.; Kuperman, Marina; Potocki, Sławomir; Gumienna‐Kontecka, Elżbieta; Жданов, А. П.; Yarmoluk, S. M.; Voloshin, Yan Z.; Zhizhin, K. Yu.; Кузнецов, Н. Т.; El’skaya, A. V.

doi:10.1016/j.jlumin.2015.08.042

Cited by 37 publications

(16 citation statements)

References 25 publications

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“…[13,28] For example,K uperman et al have recently investigated the binding of perhalogenated closo-borates (B 10 X 10 2À and B 12 X 12 2À ;X :C l, Br,a nd I) to bovine and human serum albumins. [28] Them easured binding constants were higher than the values obtained with the parent hydrogen cluster [165] and varied from 10 4 to 10 6 m À1 .G oszczyń ski et al have expanded the interactions with serum albumin from dodecaborates to other hydrophobic or superchaotropic boron cluster types,n amely carboranes and metallacarboranes; [13] they established the affinity order,d odecaborate anion (B 12 H 12 2À ,s uperchaotropic) ! carborane (C 2 B 10 H 12 ,h ydrophobic) < metallacarborane ([M(C 2 B 9 H 11 ) 2 À ], superchaotropic).…”

Section: Methodsmentioning

confidence: 99%

“…[10,162] Indications of interactions of large anions with proteins were known even before their superchaotropic character had been introduced. [29,[163][164][165][166] Thec lassification of dodecaborate clusters in 2015 [10] sparked several lines of follow-up work Reprinted with permission from Ref. [161].…”

Section: Biologically Relevant Interactions With Proteins Peptides mentioning

confidence: 99%

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The Chaotropic Effect as an Assembly Motif in Chemistry

2018

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Following up on scattered reports on interactions of conventional chaotropic ions (for example, I−, SCN−, ClO4 −) with macrocyclic host molecules, biomolecules, and hydrophobic neutral surfaces in aqueous solution, the chaotropic effect has recently emerged as a generic driving force for supramolecular assembly, orthogonal to the hydrophobic effect. The chaotropic effect becomes most effective for very large ions that extend beyond the classical Hofmeister scale and that can be referred to as superchaotropic ions (for example, borate clusters and polyoxometalates). In this Minireview, we present a continuous scale of water–solute interactions that includes the solvation of kosmotropic, chaotropic, and hydrophobic solutes, as well as the creation of void space (cavitation). Recent examples for the association of chaotropic anions to hydrophobic synthetic and biological binding sites, lipid bilayers, and surfaces are discussed.

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Section: Methodsmentioning

confidence: 99%

Section: Biologically Relevant Interactions With Proteins Peptides mentioning

confidence: 99%

The Chaotropic Effect as an Assembly Motif in Chemistry

2018

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“…Four main forces, namely, hydrophobic interactions, hydrogen bonding, and van der Waals and electrostatic interaction forces are involved in the ligand-protein interaction [33][34][35].…”

Section: Ermodynamic Parametersmentioning

confidence: 99%

“…e binding distance in BSA and 5d was calculated using uorescence resonance energy transfer (FRET) [34,35] ( Figure 6). FRET occurs due to an overlap in the emission spectrum (donor) and absorption spectrum (acceptor).…”

Section: Energy Transfermentioning

confidence: 99%

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Almehizia

Bakheit

Zargar

et al. 2019

Journal of Spectroscopy

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In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.

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“…Recently, the association of the hydrogen closo ‐borates [B 10 H 10 ] 2− , [B 12 H 12 ] 2− and their halogen derivatives with serum albumins was characterized ,…”

Section: Introductionmentioning

confidence: 99%

The Discovery of the Effect of closo‐Borate on Amyloid Fibril Formation

Kuperman

Chernii

Varzatskii³

et al. 2017

ChemistrySelect

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The activity of the boron cluster ‐ closo‐borates in protein amyloid fibrillization was first studied. For this, we explored the effect of dianionic compound [B12H12]2− on aggregation of amyloidogenic protein insulin by the circular dichroism spectroscopy, amyloid‐sensitive fluorescent dye based assay and transmission electron microscopy. It was shown that the presence of closo‐borate during fibrillization reaction speeds up the loss of the protein α‐helical structure. This effect of dianionic compound on protein fibrillization process is concentration‐dependent. Closo‐borate at low concentration (10 mM) enhances the intensity of insulin fibrillization, while at higher concentration (50 mM, 100 mM) fluorescent assay showed the decrease of this intensity. The morphology of fibrils formed in the presence of the boron dianion differs from that of free insulin, namely they are less branched and have the bigger diameter. Besides, closo‐borate‐induced fibrils have strong proneness to stick together forming large aggregated clots.

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An interaction of the functionalized closo -borates with albumins: The protein fluorescence quenching and calorimetry study

Cited by 37 publications

References 25 publications

The Chaotropic Effect as an Assembly Motif in Chemistry

The Chaotropic Effect as an Assembly Motif in Chemistry

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

The Discovery of the Effect of closo‐Borate on Amyloid Fibril Formation

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