Study on the structural changes of bovine serum albumin with effects on polydatin binding by a multitechnique approach

Peng, Xialian; Yao, Di; Pan, Ying‐Ming; Yu, Qing; Ni, Shouhai; Bian, He‐Dong; Huang, Fu‐Ping; Liang, Hong

doi:10.1016/j.saa.2011.06.003

Cited by 15 publications

(15 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The characteristic peaks near 1,633.37, 1,618.17, and 1,248.05/cm can be attributed to the amide I, II, and III bonds of BSA or RGD, respectively (the inset in Figure b,c‐1) (Schweitzer‐Stenner et al, ; Yin, Bi, & Gan, ). The absorption peak in the interval 500–550/cm is the disulfide bridge (SS) absorption peak and FeO stretching vibration of BSA/Mal‐SPIONs (Figure c‐2) (Peng et al, ; Qian & Krimm, ). The results of FTIR show that RGD or BSA has been successfully connected to the surface of Mal‐SPIONs.…”

Section: Resultsmentioning

confidence: 99%

Subcellular distributions of iron oxide nanoparticles in rat brains affected by different surface modifications

Wang

Zhang

et al. 2019

J Biomedical Materials Res

View full text Add to dashboard Cite

The impact of the surface modification on the subcellular distribution of nanoparticles in the brain remains elusive. The nanoparticles prepared by conjugating polyethylene glycol and maleic anhydride‐coated superparamagnetic iron oxide nanoparticles (Mal‐SPIONs) with bovine serum albumin (BSA/Mal‐SPIONs) and with Arg–Gly–Asp peptide (RGD/Mal‐SPIONs) were injected into the rat substantia nigra. Observation of transmission electron microscopy (TEM) samples obtained 24 h after perfusion showed that abundant RGD/Mal‐SPIONs accumulated in the myelin sheath, dendrites, axon terminals and mitochondria, and on cell membranes in the brain tissue near the injection site. For rats injected with BSA/Mal‐SPIONs, a few nanoparticles accumulated in the myelin sheath, axon terminals, endoplasmic reticulum, mitochondria, Golgi, and lysosomes of neurons and glial cells while least SPIONs in rats injected with Mal‐SPIONs were found. TEM pictures showed some Mal‐SPIONs were expelled out of the brain. RGD/Mal‐SPIONs diffused extensively to the thalamus, frontal cortex, temporal lobe, olfactory bulb, and brain stem after injection. Only a few BSA/Mal‐SPIONs diffused to the afore‐mentioned brain areas. This work reveals different surface modifications on the iron oxide nanoparticles play crucial roles in their distribution and diffusion in the rat brains.

show abstract

Section: Resultsmentioning

confidence: 99%

Subcellular distributions of iron oxide nanoparticles in rat brains affected by different surface modifications

Wang

Zhang

et al. 2019

J Biomedical Materials Res

View full text Add to dashboard Cite

show abstract

“…Based on previous studies , the band range from 1640 to 1610 cm –1 was usually assigned to the β‐sheet and 1660–1650 cm –1 to the α‐helix. According to Fig.…”

Section: Resultsmentioning

confidence: 99%

Different spectroscopic and molecular modeling studies on the interaction between cyanidin‐3‐O‐glucoside and bovine serum albumin

Tang

Zhang

et al. 2013

Luminescence

View full text Add to dashboard Cite

Anthocyanin is one of the flavonoid phytopigments that shows strong antioxidant activity. The cyanidin-3-O-glucoside (C3G) is one of the principal types of anthocyanins. To understand the interaction between C3G and bovine serum albumin (BSA), fluorescence spectroscopy, ultraviolet-visible absorption, Fourier transform infrared spectroscopy, circular dichroism and molecular modeling techniques were used. Binding constant (K(a)) and the number of binding sites (n) were calculated. The quenching mechanism of fluorescence of BSA by C3G was discussed. The results studied by Fourier transform infrared spectroscopy and circular dichroism experiments indicate that the secondary structures of the protein have been changed by the interaction of C3G with BSA. The result of molecular modeling confirmed that the C3G bound to the site I (sub-domain IIA) of BSA, and that the hydroxyl groups in the B ring of C3G took part in the binding with BSA.

show abstract

“…In this study, FTIR, a widely used technique for determining secondary structure of protein, was applied to investigate the conformational changes of BSA during the preparation of electrospun fiber mat. Common features of protein’s FTIR spectra are the amide bands, among which the amide I band (1700–1600 cm –1 ) is the most useful one in the analysis of protein secondary structure . Generally, the peaks between 1660 and 1650 cm –1 are considered to be characteristics of α-helical structure; peaks ranging from 1640–1610 cm –1 represent β-sheet; the peaks from 1660–1700 cm –1 and 1640–1650 cm –1 are assigned to β-turns and random coil conformation, respectively .…”

Section: Resultsmentioning

confidence: 99%

“…Common features of protein’s FTIR spectra are the amide bands, among which the amide I band (1700–1600 cm –1 ) is the most useful one in the analysis of protein secondary structure . Generally, the peaks between 1660 and 1650 cm –1 are considered to be characteristics of α-helical structure; peaks ranging from 1640–1610 cm –1 represent β-sheet; the peaks from 1660–1700 cm –1 and 1640–1650 cm –1 are assigned to β-turns and random coil conformation, respectively . By adding the peak areas assigned to particular secondary structure elements, it was found that the native BSA contained 42.5% α-helix, 11.3% β-sheet, 21.4% β-turn, and 24.8% random coil structures, suggesting that the secondary structures of BSA were dominated by α-helix conformation (Figure ).…”

Section: Resultsmentioning

confidence: 99%

Preparation and Characterization of Protein-Loaded Electrospun Fiber Mat and Its Release Kinetics

Wen

Huang

et al. 2017

J. Agric. Food Chem.

View full text Add to dashboard Cite

For the enhancement of protein's bioavailability, a specific delivery system was developed by coaxial electrospinning. Bovine serum albumin (BSA) was used as protein model, and the core-sheath fiber mat was fabricated using sodium alginate as shell layer and the BSA-loaded chitosan nanoparticle that was prepared previously as core layer. By optimizing electrospinning parameters, uniform fibers with diameters ranging from 200-600 nm were obtained, and transmission electron microscopy and confocal laser scanning microscopy revealed their core-sheath structures. Fourier transform infrared spectroscopy (FTIR) analysis demonstrated that there existed molecular interaction between components, which enhanced the mat's thermal stability and mechanic property. It was found that the predominant release mechanism of BSA from fiber mat was erosion, and little change occurred in the secondary structure of encapsulated BSA indicated by FTIR and circular dichroism analysis. The study shows that the obtained fiber mat is a potential delivery system for protein.

show abstract

Study on the structural changes of bovine serum albumin with effects on polydatin binding by a multitechnique approach

Cited by 15 publications

References 29 publications

Subcellular distributions of iron oxide nanoparticles in rat brains affected by different surface modifications

Subcellular distributions of iron oxide nanoparticles in rat brains affected by different surface modifications

Different spectroscopic and molecular modeling studies on the interaction between cyanidin‐3‐O‐glucoside and bovine serum albumin

Preparation and Characterization of Protein-Loaded Electrospun Fiber Mat and Its Release Kinetics

Contact Info

Product

Resources

About