Determination of Albumin in Bronchoalveolar Lavage Fluid by Flow-Injection Fluorometry Using Chromazurol S

Sato, Takaaki; Saito, Yoshihiro; Chikuma, Masahiko; Saito, Yutaka; Nagai, Sonoko

doi:10.1248/bpb.31.336

Cited by 6 publications

(4 citation statements)

References 14 publications

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“…This is quite a relevant information showing how the same agonist can be judged to be dysopsonic or opsonic depending on the physical-chemical characteristics of the pristine NP surface. Ruge et al ( 74 ) showed that purified SP-A at 10 μg/ml (compatible with BALF SP-A concentration, see ( 75 ), mediated the association to alveolar macrophages of magnetite NPs (110–180 nm) coated with different polymers and molecules (starch, carboxymethyldextran, chitosan, poly-maleic-oleic acid, phosphatidylcholine) which was significantly stronger than that observed in the presence of a concentration of BSA (1 mg/ml) indeed much greater than that measured in BALF ( 76 ). Mannosilated PEG chains grafted on NPs improved TPH1 macrophage cell capture in the presence of purified SP-A ( 77 ).…”

Section: Influence On Np-cell Interactions Of Specific Np-bound Protementioning

confidence: 75%

Opsonins and Dysopsonins of Nanoparticles: Facts, Concepts, and Methodological Guidelines

2020

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Understanding the effects mediated by a set of nanoparticle (NP)-bound host biomolecules, often indicated with the umbrella term of NP corona , is essential in nanomedicine, nanopharmacology, and nanotoxicology. Among the NP-adsorbed proteome , some factors mediate cell binding, endocytosis, and clearing by macrophages and other phagocytes (opsonins), while some others display few affinities for the cell surface (dysopsonins). The functional mapping of opsonins and dysopsonins is instrumental to design long-circulating and nanotoxicologically safe next-generation nanotheranostics. In this review, we critically analyze functional data identifying specific proteins with opsonin or dysopsonin properties. Special attention is dedicated to the following: (1) the simplicity or complexity of the NP proteome and its modulation, (2) the role of specific host proteins in mediating the stealth properties of uncoated or polymer-coated NPs, and (3) the ability of the innate immune system, and, in particular, of the complement proteins, to mediate NP clearance by phagocytes. Emerging species-specific peculiarities, differentiating humans from preclinical animal models (the murine especially), are highlighted throughout this overview. The operative definition of opsonin and dysopsonin and the measurement schemes to assess their in vitro efficacy is critically re-examined. This provides a shared and unbiased approach useful for NP opsonin and dysopsonin systematic identification.

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Section: Influence On Np-cell Interactions Of Specific Np-bound Protementioning

confidence: 75%

Opsonins and Dysopsonins of Nanoparticles: Facts, Concepts, and Methodological Guidelines

2020

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“…The spectral changes observed on the binding of fluorophores with proteins are important tools for the investigations of the topology of the binding sites, of the conformational changes and for the characterization of substrate to ligand binding [ 1 ]. The determination of protein quantity in biological liquids is of great importance in biology and medicine [ 2 ] and fluorescent probes are successfully applied for this approach [ 3 ]. Serum albumin being the major transporters binding protein for the drugs and other physiological substances, it is considered as a model for studying drug–protein interaction in vitro .…”

Section: Introductionmentioning

confidence: 99%

Bovine and Human Serum Albumin Interactions with 3-Carboxyphenoxathiin Studied by Fluorescence and Circular Dichroism Spectroscopy

2010

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The interactions of 3-carboxyphenoxathiin with Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA) have been studied by fluorescence and circular dichroism spectroscopy. The binding of 3-carboxyphenoxathiin quenches the BSA and HSA fluorescence, revealing a 1:1 interaction with a binding constant of about 105 M-1. In addition, according to the synchronous fluorescence spectra of BSA and HSA in presence of 3-carboxyphenoxathiin, the tryptophan residues of the proteins are most perturbed by the binding process. Finally, the distance between the acceptor, 3-carboxyphenoxathiin, and the donor, BSA or HSA, was estimated on the basis of the Förster resonance energy transfer (FRET). The fluorescence results are correlated with those obtained from the circular dichroism spectra, which reveal the change of the albumin conformation during the interaction process.

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“…The experimental results indicated that quenching of the fluorescence of BSA by febuxostat was probably followed a static as well as dynamic mechanism and the binding reaction was mainly enthalpy driven, where hydrophobic interaction played a major role. The binding nature assumed that the maximum binding occurs in the principal regions of ligand binding domain, located in hydrophobic cavities in the sub domains IIA and IIIA [5,6]. A phenomenon of mixed static and dynamic quenching was observed at both 280 and 293 nm excitation wavelength (λ ex ), whereas emission occurred at λ em =380 nm, which is careful illustrated with modified Stern-Volmer equation.…”

Section: Resultsmentioning

confidence: 97%

“…Dose and dosing interval completely depend on binding of drugs with different protein in the body. Quantification of circulating protein is always having a great importance in biology and medicine to understand and minimize the unwanted side effect of drug [6]. Escalating apparent solubility of hydrophobic drugs with the modulation pattern of bindings also plays a vital role in the delivery of drugs into the cell.…”

Section: Introductionmentioning

confidence: 99%

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

Rabbi¹,

Didaruzzaman²,

Sultan³

2015

J Bioanal Biomed

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Citation: Rabbi SNI, Sultan MdZ, Sohel MdD, Sultan MdZ (2015) Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy. J Bioanal Biomed 7: 164-170. doi:10.4172/1948-593X.1000138 Copyright: © 2015 Rabbi SNI, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. AbstractThe interaction of an anti-gout drug, febuxostat was studied with bovine serum albumin (BSA) applying fluorescence quenching method for the first time. Interaction parameter and magnitude of the force indicated for both, dynamic and static quenching in between febuxostat and BSA protein. Thermodynamic studies indicated for both hydrogen and hydrophobic interactions, observed at 280 nm and only hydrophobic at 293 nm excitation wavelength. Negative ΔH o and positive ΔS o , indicated for distinctive characteristics for the existence of both, hydrogen and hydrophobic binding throughout the interactions. The binding constant K b at λ ex =280 nm was 3.467 × 10 3 µM -1 and 4.943 × 10 3 µM -1 at 298 and 308 K temperature whereas, 5.54 × 10 3 µM -1 and 4.44 × 10 3 µM -1 was noted during excitation at λ ex =293 nm wavelength. The K b values in different temperatures assumed that the stability of binding increased with the increase of temperature at λ ex =280 nm, but reverse effect was experienced at an excitation wavelength of λ ex =293 nm. The number of bound febuxostat molecules per BSA protein was found ~1.5 at both 298 and 308 K. Study of Interaction between

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Determination of Albumin in Bronchoalveolar Lavage Fluid by Flow-Injection Fluorometry Using Chromazurol S

Cited by 6 publications

References 14 publications

Opsonins and Dysopsonins of Nanoparticles: Facts, Concepts, and Methodological Guidelines

Opsonins and Dysopsonins of Nanoparticles: Facts, Concepts, and Methodological Guidelines

Bovine and Human Serum Albumin Interactions with 3-Carboxyphenoxathiin Studied by Fluorescence and Circular Dichroism Spectroscopy

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

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