2015
DOI: 10.1016/j.ijbiomac.2015.04.028
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Interaction of bovine serum albumin with starch nanoparticles prepared by TEMPO-mediated oxidation

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Cited by 16 publications
(6 citation statements)
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“…The emission intensity of Trp decreases with an increase in ZnO NPs concentration which indicates quenching of the intrinsic HSA fluorescence by ZnO NPs. Previous works have reported similar quenching on the interaction of proteins with NPs [26,29] . According to the Stern-Volmer plot (Figure 1e), the plot of F0/F against [Q] is a straight line and slope of line is KSV.…”
Section: Fluorimetric Analysessupporting
confidence: 58%
See 1 more Smart Citation
“…The emission intensity of Trp decreases with an increase in ZnO NPs concentration which indicates quenching of the intrinsic HSA fluorescence by ZnO NPs. Previous works have reported similar quenching on the interaction of proteins with NPs [26,29] . According to the Stern-Volmer plot (Figure 1e), the plot of F0/F against [Q] is a straight line and slope of line is KSV.…”
Section: Fluorimetric Analysessupporting
confidence: 58%
“…This residue is highly sensitive to its local micro-environment and a trivial change in the local environment either by ligand binding or conformational changes would significantly quench it [9,25] . Phenylalanine has a very low quantum yield and the fluorescence of tyrosine can be quenched if it's ionized or placed near an amino group, a carboxyl group or a tryptophan [28,29] . For identifying variations in HSA folding, fluorescence emission spectra of tryptophan in absence and presence of ZnO NPs were measured using fluorescence spectroscopy (Figure 1d).…”
Section: Fluorimetric Analysesmentioning
confidence: 99%
“…Bovine serum albumin (BSA) has structural homology with human serum albumin and has been extensively studied. Ji, Qiu, Li, Xiong, and Sun (2015) and Fan, Ji, Zhao, Xiong, and Sun (2015) found that BSA interacted with SNPs through electrostatic interaction and hydrophobic interaction. The BSA helix content was reduced and the conformation of BSA became more compact.…”
Section: Interaction Between Starch‐based Nanoparticles and Food Compmentioning
confidence: 99%
“…Inside of the blood vessel, by exposure of the blood proteins to QDs, these proteins may be adsorbed on the QDs surface, leading to the formation of the protein-QDs conjugates [13][14][15][16]. The attached proteins at the surface of QDs (protein corona) undergo some structural changes, and produce the protein aggregates or some toxic proteins [17,18]. On the other hand, formation of the protein corona at the surface of QDs may alter the normal function of the QDs and also may change the selective binding of the QD-bioconjugates to their intended target or even in some cases may deliver the QD-bioconjugates to other (unrelated) parts of body, and by this way produces various side effects [19,20].…”
Section: Introductionmentioning
confidence: 99%