The protective effects of osmolytes on arginine kinase unfolding and aggregation

Xia, Yong; Park, Yong‐Doo; Mu, Hang; Zhou, Hai‐Meng; Wang, Xiaoyun; Meng, Fanyue

doi:10.1016/j.ijbiomac.2006.10.004

Cited by 56 publications

(28 citation statements)

References 36 publications

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“…Yancey et al [31] showed that the activity and stability of certain enzymes were perturbed by arginine and concluded that arginine is a protein-destabilizer. Xia et al [32] have made a similar observation and showed that fluorescence properties of aminoacylase are perturbed by arginine. They interpreted the observed effects of arginine in terms of denaturing property of the guanidinium group, which makes guanidine hydrochloride (Gn-HCl) a strong denaturant.…”

Section: Arginine (Arg)mentioning

confidence: 75%

“…Later, proline was found to prevent aggregation during hen egg-white lysozyme refolding. Also proline has been used during refolding of arginine kinase [32] and aminoacylase [51]. Proline inhibits protein aggregation by 50 Temperature Carbonic anhydrase [13,14] Poly(N-isopropylacrylamide) Temperature Carbonic anhydrase lysozyme [15,16] binding to folding intermediates.…”

Section: Proline (Pro)mentioning

confidence: 99%

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Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Alibolandi¹,

Mirzahosei²

2011

American J. of Biochemistry and Molecular Biology

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Escherichia coli is one of the most widely used hosts for the production of recombinant proteins but insoluble expression of heterologous proteins is a major bottleneck in production of recombinant proteins in E. coli. In vitro refolding of inclusion body into proteins with native conformations is a solution for this problem but there is a need for optimization of condition for each protein specifically. Several approaches have been described for in vitro refolding; most of them involve the use of additives for assisting correct folding. Cosolutes play a major role in refolding process and can be classified according to their function as aggregation suppressors and folding enhancers. This paper presents a review of additives that are used in refolding process of insoluble recombinant proteins in small scale and industrial processes.

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Section: Arginine (Arg)mentioning

confidence: 75%

Section: Proline (Pro)mentioning

confidence: 99%

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Alibolandi¹,

Mirzahosei²

2011

American J. of Biochemistry and Molecular Biology

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“…181 A major category of these neutral compounds is sugars/polyols. These sugars/polyols normally have a stabilization effect and inhibit protein aggregation under different experimental conditions.…”

Section: Small Neutral Additivesmentioning

confidence: 99%

“…They can help to maintain the correct conformation of proteins, which enables them to be called chemical chaperones or to be more widely recognized as osmolytes. 181,182 Many proteins are stabilized by these compounds, which differ from traditional chaperones, in that they possess limited or no specifi c molecular recognition for facilitation of protein folding. For example, the rate of aggregation of IFN -tau at 50 ° C was reduced gradually with increasing sucrose concentrations at 0.25, 0.5, 0.75, and 1.0 M. 31 Sucrose at 10% reduced the amount of HMW aggregates to a signifi cant degree during elution of a Fc fusion protein at pH 3.6.…”

Section: Small Neutral Additivesmentioning

confidence: 99%

“…182 These sugars/polyols also protect proteins under different processing or even culturing conditions. Xia et al 181 demonstrated that addition of sucrose at 0.5 M almost completely suppressed the aggregation of arginine kinase during refolding at 25 ° C. Beranger et al 183 demonstrated that trehalose treatment of prion -infected cells decreased the size of de novo produced PrP Sc aggregates, while treatment with glucose did not have this effect. It also signifi cantly protected prion -infected cells from induced oxidative damage.…”

Section: Small Neutral Additivesmentioning

confidence: 99%

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External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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Protein and Peptide Formulation Development

Ohtake¹,

Wang²

2013

Pharmaceutical Sciences Encyclopedia

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Proteins/peptides are generally much more sensitive to process‐ or storage‐induced degradations than small synthetic molecules. Therefore, significant efforts are needed to formulate these protein/peptide drug candidates into viable commercial products.This chapter reviews the degradation processes in proteins/peptides, describes factors affecting protein/peptide stability, and discusses strategies in the successful development and manufacturing of protein/peptide commercial products.

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The protective effects of osmolytes on arginine kinase unfolding and aggregation

Cited by 56 publications

References 36 publications

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

External Factors Affecting Protein Aggregation

Protein and Peptide Formulation Development

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