Secondary structure investigation of bovine serum albumin (BSA) by Fourier transform infrared (FTIR) spectroscopy in the amide III region

Li, Dongmin; Zhang, Hong; Ma, Gang

doi:10.5155/eurjchem.5.2.287-290.1007

Cited by 5 publications

(5 citation statements)

References 13 publications

(23 reference statements)

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“…After reaction, the intensity of the peaks at 1612 cm −1 and 1416 cm −1 was greatly weakened due to the cross-linking reaction. 61 A new peak appearing at 1632 cm −1 could be attributed to the vibration of the amide bond (CvO stretching (amide I)), 67,77 signal intensity by dephasing the transverse magnetization and reducing the value of the transverse relaxation time (T 2 ). The T 2 relaxation times of the AG/PEI-Fe 3 O 4 NGs in aqueous suspension at different Fe concentrations were measured and the transverse relaxivity (r 2 , the transverse relaxation rate per mM of Fe) was calculated (Fig.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of iron oxide nanoparticles within alginate nanogels for enhanced MR imaging applications

et al. 2016

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We report the design of iron oxide (Fe3O4) nanoparticle (NP)-immobilized alginate (AG) nanogels (NGs) as a novel contrast agent for enhanced magnetic resonance (MR) imaging applications. In this study, an aqueous solution of AG activated by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride was double emulsified to form NGs, followed by in situ cross-linking with polyethyleneimine (PEI)-coated Fe3O4 NPs (PEI-Fe3O4 NPs). The resultant Fe3O4 NP-immobilized AG NGs (AG/PEI-Fe3O4 NGs) were characterized via different techniques. Our results reveal that the hybrid NGs with a size of 186.1 ± 33.1 nm are water dispersible, colloidally stable, and cytocompatible in the given concentration range. Importantly, these NGs have a high r2 relaxivity (170.87 mM(-1) s(-1)) due to the high loading of Fe3O4 NPs within the NGs, and can be more significantly uptaken by cancer cells when compared with carboxylated Fe3O4 NPs. The formed AG/PEI-Fe3O4 NGs are able to be used as an effective contrast agent for the MR imaging of cancer cells in vitro and the xenografted tumor model in vivo after intravenous injection. The developed AG/PEI-Fe3O4 NGs may hold great promise for use as a novel contrast agent for the enhanced MR imaging of different biological systems.

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Section: Resultsmentioning

confidence: 99%

Immobilization of iron oxide nanoparticles within alginate nanogels for enhanced MR imaging applications

et al. 2016

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“…The amide I–III bands, including the secondary structure of protein molecules, can be very sensitive to detect. The amide I region is often used in quantitative analysis of the secondary structure with the second derivative, deconvolution, and curve fitting [26,27,28,29,30]. The structural changes in fibroin can be analyzed according to the crystallinity obtained by X-ray diffraction [31,32] and differential scanning calorimetry.…”

Section: Introductionmentioning

confidence: 99%

Microstructure Transitions and Dry-Wet Spinnability of Silk Fibroin Protein from Waste Silk Quilt

Zhang

Pan

2019

Polymers

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With excellent biocompatibility and biodegradability, silk fibroin has been developed into many protein materials. For producing regenerated silk fibroin (RSF) fibers, the conformation transition of silk fibroin needs to be thoroughly studied during the spinning process. Since the many silk fabrics that are discarded comprise an increasing waste of resources and increase the pressure on the environment, in this paper, waste silk fiber was recycled in an attempt to prepare regenerated fibroin fiber by dry-wet spinning. Ethanol was the coagulation bath. The rheological properties of all the RSF solutions were investigated to acquire rheology curves and non-Newtonian indexes for spinnability analysis. Four stages of the spinning process were carried out to obtain RSF samples and study their conformation transitions, crystallization, and thermal properties by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction, and differential scanning calorimetry. Quantitative analysis of the FTIR results was performed to obtain specific data regarding the contents of the secondary structures. The results showed that higher concentration spinning solutions had better spinnability. As the spinning process progressed, random coils were gradually converted into β-sheets and crystallization increased. Among the different influencing factors, the ethanol coagulation bath played a leading role in the conformation transitions of silk fibroin.

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“…As a result, the CAP-IDAN molecules become more mobile and more of them penetrate into the protein pocket, causing an increase in the τ 1 of dye molecules (figure 2, curve 1). The native structure of the α-helix is destroyed and a disordered protein structure appears at the increasing value of pH (at pH > 5.0) [25]. As a result, a decrease of τ 1 is observed (figure 2, curve 1).…”

Section: Investigation Of the Spectral-kinetic Characteristics Of Cap...mentioning

confidence: 96%

The binding of bovine serum albumin with dye molecules at different pH values. Fluorescence lifetime studies

et al. 2021

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The spectral and kinetic characteristics of the fluorescence of the solutions of bovine serum albumin (BSA) and the dyes (N-(p-carboxyphenyl) imide of 4-(dimethylamino) naphthalic acid (CAPIDAN) and Bengal Rose (BR)) in BSA solutions were studied at 3.5 < pH < 8.0. It was discovered that the attenuation of CAPIDAN fluorescence at the studied pH region is described by the sum of three components (with the values of time constants: 6.0 ns < τ 1 < 8.5 ns, 1.8 ns < τ 2 < 2.2 ns, 0.4 ns < τ 3 < 0.6 ns), while it is described by two components for BR (0.33 ns < τ 1 < 0.4 ns, 2.0 ns < τ 2 < 3.1 ns). It is shown that the mechanisms of the binding of dye and protein molecules are different for CAPIDAN and BR. The binding process of CAPIDAN and BSA is regulated by the conformation of the binding center. The interaction between the BR and BSA molecules is electrostatic, the magnitude of this interaction is determined by the ratio of the charges of the dye and protein molecules. The dependence of the wavelength of the maximum of the spectra, the intensity of the glow and the efficiency of quenching of the fluorescence of the molecules of the studied dyes on the pH is analyzed. The parameters dμ, which characterizes the change in the dipole moment of the fluorophore during its excitation, and η, which characterizes the change in the intensity at the maximum of the fluorescence spectrum at different pH solutions, were also determined for BR. The following ratios were determined at the studied pH range: d μ > 1 and η < 1. The changes of the characteristics of the stationary fluorescence of the studied dyes at different pH of BSA solutions confirm the mechanisms of the binding between CAPIDAN or BR molecules and protein molecules.

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Secondary structure investigation of bovine serum albumin (BSA) by Fourier transform infrared (FTIR) spectroscopy in the amide III region

Cited by 5 publications

References 13 publications

Immobilization of iron oxide nanoparticles within alginate nanogels for enhanced MR imaging applications

Immobilization of iron oxide nanoparticles within alginate nanogels for enhanced MR imaging applications

Microstructure Transitions and Dry-Wet Spinnability of Silk Fibroin Protein from Waste Silk Quilt

The binding of bovine serum albumin with dye molecules at different pH values. Fluorescence lifetime studies

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