Effects of pH and protein conformation on in-solution complexation between bovine α-lactalbumin and oleic acid: Binding trend analysis by using SPR and ITC

Park, Yong Jun; Kim, Ki Hyung; Lim, Dong Woo; Lee, E.K.

doi:10.1016/j.procbio.2015.05.018

Cited by 14 publications

(7 citation statements)

References 32 publications

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“…This naturally occurs as a function of pH with the different conformations of BSA 15,16 and may also occur as a result of adsorption. 13,27 This suggests that although the isoelectric point may mediate protein adsorption as a function of pH, [34][35][36][37]48,50 there are also other effects driving nanoparticle-protein interactions. At pH 2.0, the greatest change in the alpha-helix content is observed.…”

Section: Protein Secondary Structure As a Function Of Phmentioning

confidence: 99%

“…13,27 The adsorption of proteins, including BSA, on nanoparticle surfaces has been investigated in terms of impacts on nanoparticle aggregation, protein coverage, and protein structure. [27][28][29][30][31][32][33] Investigations on the effects of pH have been conducted and shown that protein adsorption is the greatest at or near the isoelectric point, [34][35][36][37] and there is not necessarily a pH-dependent trend for protein adsorption to nanoparticle surfaces away from the isoelectric point. 37 Aggarwal et al conducted a study on pure silica and zirconia nanoparticle surfaces and a mixture of nanoparticle surfaces and found that the composite surface better retains the native protein structure upon adsorption.…”

Section: Introductionmentioning

confidence: 99%

“…41,42 pH-dependent studies of proteins on nanoparticle surfaces have indicated that the isoelectric point of the protein corresponds to the greatest adsorption onto the nanoparticle surface, independent of the point of zero charge for the nanoparticle substrate. [34][35][36][37] However, other studies indicate that the isoelectric point of the substrate determines maximum protein adsorption. 48,50 Quantification of protein adsorption has been done in the past using ATR-FTIR spectroscopy in an equilibrium state; however, here we use thermogravimetric analysis (TGA) to determine the number of protein molecules which adsorb to a nanoparticle surface.…”

Section: Introductionmentioning

confidence: 99%

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Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

et al. 2017

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Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO2) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO2 nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO2 nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO2 nanoparticles, whereas for SiO2 nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO2 complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO2 complex with a value of ca. 3 ± 1 × 1011 molecules cm−2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein–nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).

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Section: Protein Secondary Structure As a Function Of Phmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

et al. 2017

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“…[11,12] These interactions can be affected by a variety of factors including temperature, [4, 13, 14, 15] pH, [16, 17, 18] ionic strength, [19] solvent, [20, 21, 22] surface effects, [23] as well as instrumental parameters[24]. Most methods intended to change protein conformation involve bulk solution manipulations, such as the addition of acid, base, organic solvent, supercharging reagents[14] or other additives, as well as heating.…”

Section: Introductionmentioning

confidence: 99%

Joule Heating and Thermal Denaturation of Proteins in Nano-ESI Theta Tips

Zhao

Matt

et al. 2017

J. Am. Soc. Mass Spectrom.

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Electroosmotically-induced Joule heating in theta tips and its effect on protein denaturation were investigated. Myoglobin, equine cytochrome c, bovine cytochrome c and carbonic anhydrase II solutions were subjected to electroosmosis in a theta tip and all of the proteins were denatured during the process. The extent of protein denaturation was found to increase with the applied square wave voltage and electrolyte concentration. The solution temperature at the end of a theta tip was measured directly by Raman spectroscopy and shown to increase with the square wave voltage, thereby demonstrating the effect of Joule heating through an independent method. The electroosmosis of a solution comprised of myoglobin, bovine cytochrome c, and ubiquitin demonstrated that the magnitude of Joule heating that causes protein denaturation is positively correlated with protein melting temperature. This allows for a quick determination of a protein’s relative thermal stability. This work establishes a fast, novel method for protein conformation manipulation prior to MS analysis and provides a temperature-controllable platform for the study of processes that take place in solution with direct coupling to mass spectrometry.

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“…The method is versatile and can be applied to many systems and conditions. Examples include GlnK and ATP binding in the presence of 2-oxoglutarate (2-OG) (Radchenko et al 2010), the effect of pH and the conformation in the complexation of bovine a-lactalbumin and oleic acid (Park et al 2015), and the toxicity of the sarafloxacin compound to the catalase enzyme (Cao et al 2013). In light of its potential, the technique deserves to be explored in the field of the freezing process.…”

Section: Introductionmentioning

confidence: 99%

Effects of freezing and the cryoprotectant lactobionic acid in the structure of GlnK protein evaluated by circular dichroism (CD) and isothermal titration calorimetry (ITC)

et al. 2016

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Freezing is a widely applied method in food preservation. The technique has negative effects on sensory and textural properties of some foods. In this study the effects of the freeze-thaw process and lactobionic acid (LBA) as a cryoprotectant on GlnK protein solution were evaluated by circular dichroism (CD) analysis and isothermal titration calorimetry (ITC). The freeze-thaw cycles caused changes in GlnK conformation and interactions with small ligands (adenosine triphosphate, ATP). CD assay demonstrated changes in the molar ellipticity values of the samples subjected to freezing, indicating conformational changes to the GlnK protein. Additionally, ITC analysis indicated that the freeze-thaw process caused changes in the interaction properties of GlnK with its ligand ATP. LBA cryoprotectant activity was also evaluated and with both of the techniques it was demonstrated that the compound prevented the damage caused by the freeze-thaw process, thereby maintaining the characteristics of the samples.

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Effects of pH and protein conformation on in-solution complexation between bovine α-lactalbumin and oleic acid: Binding trend analysis by using SPR and ITC

Cited by 14 publications

References 32 publications

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

Joule Heating and Thermal Denaturation of Proteins in Nano-ESI Theta Tips

Effects of freezing and the cryoprotectant lactobionic acid in the structure of GlnK protein evaluated by circular dichroism (CD) and isothermal titration calorimetry (ITC)

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