Molecular Characteristics of Bovine Serum Albumin-Dextran Conjugates

Jung, Seo-Jeong; Choi, Soo Jung; Kim, Hyun Jung; Moon, Tae Wha

doi:10.1271/bbb.60026

Cited by 37 publications

(22 citation statements)

References 27 publications

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“…The longer and shorter lifetimes indicated that BSA contained two tryptophan residues that fluoresced in two different environments [29] and one of the tryptophan residues in the protein may be buried inside the hydrophobic interior of protein whereas the other tryptophan residue may be close to quencher [30]. This is in good agreement with the reports that BSA has two tryptophan residues, Trp-134 in the first domain located on the surface of molecule and Trp-212 in the second domain located within a hydrophobic binding pocket [14].…”

Section: Resultssupporting

confidence: 89%

“…Thus, CeO2 nanoparticles have extensive potential as a therapeutic agent for the treatment of cancer, as well as other diseases [13]. Serum albumin, the most abundant protein found in human blood functions as a carrier for various endogenous and exogenous ligands [14]. Owing to its physiological properties, purification and stability in biochemical reactions, bovine serum albumin is widely used as a model globular protein and is an ideal protein for intrinsic fluorescence measurements due to the presence of two intrinsic tryptophan residues.…”

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confidence: 99%

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Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Abraham¹

2018

Asian J. Chem.

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Section: Resultssupporting

confidence: 89%

mentioning

confidence: 99%

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Abraham¹

2018

Asian J. Chem.

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“…The maximum°uorescence emission wavelengths of BSA and HSA centered at around 344 nm and 358 nm respectively upon excitation at 280 nm, arising from Trp°uorescence. 25 For AlPc-BSA complex as well as AlPc-HSA complex, the°uorescence intensity gradually decreased with the increase of AlPc concentrations, and a shift of the maximum emission wavelength was also observed from 344 nm to 356 nm for BSA, and from 358 nm to 380 nm for HSA. These results suggested that microenvironment of the Trp residues changed, by means of an interaction between AlPc and serum albumins (BSA and HSA), leading to a ground-state complex formation.…”

Section: A±nity Measurementsmentioning

confidence: 90%

Spectroscopic analysis of the interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanines and serum albumins

Zheng

Lin

et al. 2017

J. Innov. Opt. Health Sci.

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The binding interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanine (AlPc), and two-serum albumins (bovine serum albumin (BSA) and human serum albumin (HSA)) has been investigated. AlPc could quench the intrinsic°uorescence of BSA and HSA through a static quenching process. The primary and secondary binding sites of AlPc on BSA were domain I and III of BSA. The primary binding site of AlPc on HSA was domain I, and the secondary binding sites of AlPc on HSA were found at domains I and II. Our results suggest that AlPc readily interact with BSA and HSA implying that the amphiphilic substituents AlPc may contribute to their transportation in the blood.

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“…Maillard reaction was conducted according to previously reported protocols 22, 23 with slight modifications. Briefly, BSA and dextran (with different molecular weight) stock solutions were respectively prepared by dissolving in ultrapure water at 40 mg/mL and 100 mg/mL.…”

Section: Methodsmentioning

confidence: 99%

Synthetic surfactant- and cross-linker-free preparation of highly stable lipid-polymer hybrid nanoparticles as potential oral delivery vehicles

Wang

Xue

et al. 2017

Sci Rep

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The toxicity associated with concentrated synthetic surfactants and the poor stability at gastrointestinal condition are two major constraints for practical applications of solid lipid nanoparticles (SLN) as oral delivery vehicles. In this study, a synthetic surfactant-free and cross-linker-free method was developed to fabricate effective, safe, and ultra-stable lipid-polymer hybrid nanoparticles (LPN). Bovine serum albumin (BSA) and dextran varying in molecular weights were first conjugated through Maillard reaction and the conjugates were exploited to emulsify solid lipid by a solvent diffusion and sonication method. The multilayer structure was formed by self-assembly of BSA-dextran micelles to envelope solid lipid via a pH- and heating-induced facile process with simultaneous surface deposition of pectin. The efficiency of different BSA-dextran conjugates was systematically studied to prepare LPN with the smallest size, the most homogeneous distribution and the greatest stability. The molecular interactions were characterized by Fourier transform infrared and fluorescence spectroscopies. Both nano spray drying and freeze-drying methods were tested to produce spherical and uniform pectin-coated LPN powders that were able to re-assemble nanoscale structure when redispersed in water. The results demonstrated the promise of a synthetic surfactant- and cross-linker-free technique to prepare highly stable pectin-coated LPN from all natural biomaterials as potential oral delivery vehicles.

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Molecular Characteristics of Bovine Serum Albumin-Dextran Conjugates

Cited by 37 publications

References 27 publications

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Spectroscopic analysis of the interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanines and serum albumins

Synthetic surfactant- and cross-linker-free preparation of highly stable lipid-polymer hybrid nanoparticles as potential oral delivery vehicles

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