Arginine controls heat‐induced cluster–cluster aggregation of lysozyme at around the isoelectric point

Tomita, Shunsuke; Yoshikawa, H; Shiraki, Kentaro

doi:10.1002/bip.21637

Cited by 41 publications

(29 citation statements)

References 70 publications

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“…We have also shown that Arg enhances refolding of monomeric [10] and oligomeric proteins [19], and inhibits heat-induced aggregation [9],[10],[12],[13]. It has been suggested that such effects of Arg are due to the ability to solubilize aggregation-prone denatured proteins [20], as also indicated by the enhancement of solubility of hydrophobic small compounds by Arg [21]–[24].…”

Section: Introductionmentioning

confidence: 67%

Arginine Inhibits Adsorption of Proteins on Polystyrene Surface

et al. 2013

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Nonspecific adsorption of protein on solid surfaces causes a reduction of concentration as well as enzyme inactivation during purification and storage. However, there are no versatile inhibitors of the adsorption between proteins and solid surfaces at low concentrations. Therefore, we examined additives for the prevention of protein adsorption on polystyrene particles (PS particles) as a commonly-used material for vessels such as disposable test tubes and microtubes. A protein solution was mixed with PS particles, and then adsorption of protein was monitored by the concentration and activity of protein in the supernatant after centrifugation. Five different proteins bound to PS particles through electrostatic, hydrophobic, and aromatic interactions, causing a decrease in protein concentration and loss of enzyme activity in the supernatant. Among the additives, including arginine hydrochloride (Arg), lysine hydrochloride, guanidine hydrochloride, NaCl, glycine, and glucose, Arg was most effective in preventing the binding of proteins to PS particles as well as activity loss. Moreover, even after the mixing of protein and PS particles, the addition of Arg caused desorption of the bound protein from PS particles. This study demonstrated a new function of Arg, which expands the potential for application of Arg to proteins.

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Section: Introductionmentioning

confidence: 67%

Arginine Inhibits Adsorption of Proteins on Polystyrene Surface

et al. 2013

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“…As the figures show, the secondary structure was decreased immediately at high pH. It is noteworthy that the isoelectric point of lysozyme is at around pH 10; the condition at pH 10 is prone to aggregate lysozyme 36. Consequently, the inactivation of the alkaline condition might be related to the aggregation.…”

Section: Resultsmentioning

confidence: 91%

Protein Inactivation by Low‐temperature Atmospheric Pressure Plasma in Aqueous Solution

Takai

Kitano

Kuwabara

et al. 2011

Plasma Processes & Polymers

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Plasma medicine is an attractive new research area, but fundamental information related to plasma modification of biomacromolecules in aqueous solution remains elusive. As described herein, we investigated the chemical effects of low‐temperature atmospheric pressure plasma on protein in aqueous solution using lysozyme as a model. Plasma treatment decreased enzymatic activity and changed the secondary structure that results from the increased molecular weight of lysozyme with chemical modification. These effects arise neither from UV light nor from plasma heat, suggesting that the reactive species generated by the plasma affect lysozyme. The information presented in this paper represents a crucial first step for elucidating chemical reactions induced by plasma on proteins for biomedical applications.

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“…Among chemical chaperones arginine (Arg) is the most effective additive in suppressing heat- and dithiothreitol (DTT)-induced aggregation of proteins [26]–[31] and protein aggregation during in vitro folding [32]. It is suggested that Arg does not facilitate refolding, but can suppress aggregation of the proteins during refolding [33], [34].…”

Section: Introductionmentioning

confidence: 99%

“…Such favorable interactions should be reflected on Arg binding to protein surfaces [35]–[38]. Tomita et al [31] showed that heat-induced aggregation of lysozyme at around the isoelectric point occurred in a two-step process: formation of start aggregates, followed by further growth mediated by their sticking with diffusion-limited cluster-cluster aggregation. In the presence of Arg, the diffusion-limited regime changed to reaction-limited cluster-cluster aggregation.…”

Section: Introductionmentioning

confidence: 99%

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

et al. 2013

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The methodology for quantification of the anti-aggregation activity of protein and chemical chaperones has been elaborated. The applicability of this methodology was demonstrated using a test-system based on dithiothreitol-induced aggregation of bovine serum albumin at 45°C as an example. Methods for calculating the initial rate of bovine serum albumin aggregation (v agg) have been discussed. The comparison of the dependences of v agg on concentrations of intact and cross-linked α-crystallin allowed us to make a conclusion that a non-linear character of the dependence of v agg on concentration of intact α-crystallin was due to the dynamic mobility of the quaternary structure of α-crystallin and polydispersity of the α-crystallin–target protein complexes. To characterize the anti-aggregation activity of the chemical chaperones (arginine, arginine ethyl ester, arginine amide and proline), the semi-saturation concentration [L]0.5 was used. Among the chemical chaperones studied, arginine ethyl ester and arginine amide reveal the highest anti-aggregation activity ([L]0.5 = 53 and 58 mM, respectively).

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Arginine controls heat‐induced cluster–cluster aggregation of lysozyme at around the isoelectric point

Cited by 41 publications

References 70 publications

Arginine Inhibits Adsorption of Proteins on Polystyrene Surface

Arginine Inhibits Adsorption of Proteins on Polystyrene Surface

Protein Inactivation by Low‐temperature Atmospheric Pressure Plasma in Aqueous Solution

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

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