The effect of the N-B transition of bovine and human serum albumins on the binding sites of fluorescent probes

Seki, Takahiro; T, Akimoto; Iijima, T.

doi:10.1007/bf01412758

Cited by 4 publications

(1 citation statement)

References 21 publications

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“…The pKa of the dimethylamino group in the dansyl moiety in water or when attached to a small molecule is ~3.6 [44]. Protonation quenches its fluorescence [45; 46].…”

Section: Discussionmentioning

confidence: 99%

Design, synthesis, and evaluation of a new fluorescent probe for measuring polymyxin–lipopolysaccharide binding interactions

Soon¹,

Velkov²,

Chiu³

et al. 2011

Analytical Biochemistry

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Fluorescence assays employing semi-synthetic or commercial dansyl-polymyxin B, have been widely employed to assess the affinity of polycations, including polymyxins, for bacterial cells and lipopolysaccharide (LPS). The five primary γ-amines on diaminobutyric-acid residues of polymyxin B are potentially derivatized with dansyl-cholride. Mass spectrometric analysis of the commercial product revealed a complex mixture of di- or tetra- dansyl-substituted polymyxin B. We synthesized a mono-substituted fluorescent derivative, dansyl[Lys]1polymyxinB3. The affinity of polymyxin for purified Gram-negative LPS, and whole bacterial cells was investigated. The affinity of dansyl[Lys]1polymyxinB3 for LPS was comparable to polymyxin B and colistin, and considerably greater (kd < 1 μM) than for whole cells (kd ~6 to 12 μM). Isothermal titration calorimetric studies demonstrated exothermic enthalpically driven binding between both polymyxin B and dansyl[Lys]1polymyxinB3 to LPS, attributed to electrostatic interactions. The hydrophobic dansyl moiety imparted a greater entropic contribution to the dansyl[Lys]1polymyxinB3-LPS reaction. Molecular modeling revealed a loss of electrostatic contact within the dansyl[Lys]1polymyxinB3-LPS complex due to steric hindrance from the dansyl[Lys]1 fluorophore; this corresponded with diminished antibacterial activity (MIC ≥ 16 μg/mL). Dansyl[Lys]1polymyxinB3 may prove useful as a screening tool for drug development.

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“…The pKa of the dimethylamino group in the dansyl moiety in water or when attached to a small molecule is ~3.6 [44]. Protonation quenches its fluorescence [45; 46].…”

Section: Discussionmentioning

confidence: 99%

Design, synthesis, and evaluation of a new fluorescent probe for measuring polymyxin–lipopolysaccharide binding interactions

Soon¹,

Velkov²,

Chiu³

et al. 2011

Analytical Biochemistry

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The reorganization of conformations, stability and aggregation of serum albumin isomers through the interaction of glycopeptide antibiotic teicoplanin: A thermodynamic and spectroscopy study

Muthu

Jadav

Srivastava

et al. 2020

International Journal of Biological Macromolecules

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Distinguishing the transitions of fluorescence spectra of tryptophan-134 and 213 in BSA induced by bindings of UV filters, oxybenzone-3, and avobenzone

Minamide,

Tsurushima,

Koga

et al. 2024

Bulletin of the Chemical Society of Japan

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Oxybenzone-3 (OBZ) and avobenzone (ABZ), commercially available ultraviolet-light filters for sunscreens, are known to induce photosensitizing allergy as an adverse effect, similar to an analgesic ketoprofen (KTP) due to their benzophenone moiety. The present study focused on OBZ and ABZ's protein binding compared to the related analgesics, KTP, diclofenac (DCF), and ibuprofen (IBP). The bovine serum albumin (BSA) was used as a protein model, measuring the fluorescent spectral peak shifts (i) and Stern–Volmer analysis (i) of its intrinsic tryptophans. Moreover, their adsorption types (iii) were verified using the singular value decomposition (SVD) computation of fluorescence spectra. For (i), (ii), and (iii), KTP and DCF caused a no-shift peak, an ordinary dynamic quenching, and a simple Langmuir adsorption. We found OBZ exhibiting (i) red-shift and (ii) including static quenching, ABZ suggesting (i) blue-shift and (iii) binding to multiple bind sites, and IBP indicating (i) blue-shift and (iii) multivalent bindings. Integrating the results, it can be understood that OBZ interacts with subdomain IA (around W134) in BSA, while ABZ interacts with subdomain IIA (around W213) in BSA. Moreover, IBP is bound to BSA with a cooperative effect, certified by Hill's plot. OBZ and ABZ had their individual binding sites on a protein, suggesting the exchange between OBZ and ABZ might reduce their own adverse effect. The present study verified the effectiveness of the SVD computation in distinguishing the details of the adsorption manner of ligands around the intrinsic fluorescent probes.

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The effect of the N-B transition of bovine and human serum albumins on the binding sites of fluorescent probes

Cited by 4 publications

References 21 publications

Design, synthesis, and evaluation of a new fluorescent probe for measuring polymyxin–lipopolysaccharide binding interactions

Design, synthesis, and evaluation of a new fluorescent probe for measuring polymyxin–lipopolysaccharide binding interactions

The reorganization of conformations, stability and aggregation of serum albumin isomers through the interaction of glycopeptide antibiotic teicoplanin: A thermodynamic and spectroscopy study

Distinguishing the transitions of fluorescence spectra of tryptophan-134 and 213 in BSA induced by bindings of UV filters, oxybenzone-3, and avobenzone

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