Effect of 2‐hydroxypropyl‐β‐cyclodextrin on thermal stability and aggregation of glycogen phosphorylase <i>b</i> from rabbit skeletal muscle

Eronina, Tatiana B.; Chebotareva, Natalia A.; Kleymenov, Sergey Y.; Roman, Svetlana G.; Makeeva, Valentina F.; Bi, Kurganov

doi:10.1002/bip.21508

Cited by 17 publications

(13 citation statements)

References 38 publications

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“…Thus we infer that the formation of the start aggregates proceeds on the all-or-none principle. This pattern was demonstrated for thermal aggregation of β L -crystallin from bovine lens [12], [37], GAPDH from rabbit skeletal muscle [6], [23], [35], [37], [43], yeast alcohol dehydrogenase I [26], [37], tobacco mosaic virus coat protein [37], [44], Ph b from rabbit skeletal muscle [5], [23], [29], [37], [43], [45], aspartate aminotransferase from pig heart mitochondria [46] and creatine kinase from rabbit skeletal muscle [7]. On the basis of these experimental data a new model of protein aggregation was proposed [12], [23], [36], [37].…”

Section: Resultsmentioning

confidence: 84%

“…Our investigations have shown that Ph b is a convenient model for testing the compounds affecting protein denaturation and aggregation [4], [5], [25], [29], [45], [57]–[60]. Fig.…”

Section: Resultsmentioning

confidence: 99%

“…11) is accompanied by the decrease in the T 0 value to 46.1°C and the increase in parameter K agg to (3.27±0.03)⋅10 5 (counts/s)⋅(°C) −2 . This action of HP-β-CD is caused by the destabilization of the Ph b molecule as a result of binding of HP-β-CD to the native form of the enzyme and early intermediates of Ph b unfolding as suggested by the data on the kinetics of thermal inactivation and DSC data [45]. It is known that osmolytes stabilize the protein structure [61]–[63].…”

Section: Resultsmentioning

confidence: 99%

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A Protein Aggregation Based Test for Screening of the Agents Affecting Thermostability of Proteins

et al. 2011

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To search for agents affecting thermal stability of proteins, a test based on the registration of protein aggregation in the regime of heating with a constant rate was used. The initial parts of the dependences of the light scattering intensity (I) on temperature (T) were analyzed using the following empiric equation: I = K agg(T−T 0)2, where K agg is the parameter characterizing the initial rate of aggregation and T 0 is a temperature at which the initial increase in the light scattering intensity is registered. The aggregation data are interpreted in the frame of the model assuming the formation of the start aggregates at the initial stages of the aggregation process. Parameter T 0 corresponds to the moment of the origination of the start aggregates. The applicability of the proposed approach was demonstrated on the examples of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscles and bovine liver glutamate dehydrogenase studied in the presence of agents of different chemical nature. The elaborated approach to the study of protein aggregation may be used for rapid identification of small molecules that interact with protein targets.

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Section: Resultsmentioning

confidence: 84%

“…Our investigations have shown that Ph b is a convenient model for testing the compounds affecting protein denaturation and aggregation [4], [5], [25], [29], [45], [57]–[60]. Fig.…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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A Protein Aggregation Based Test for Screening of the Agents Affecting Thermostability of Proteins

et al. 2011

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“…(3) for the description of the initial parts of the kinetic curves of protein aggregation was demonstrated for thermal denaturation of Ph b [50], [76], [78], [79], GAPDH [80]–[82] and creatine kinase (CK) [83]from rabbit skeletal muscles and DTT-induced aggregation of α-lactalbumin [18] and insulin [84]. The practical significance of Eqs.…”

Section: Theory Quantification Of the Chaperone-like Activitymentioning

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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“…Among the suggested strategies to create artificial chaperones, on can mention the use polysaccharide gels [1,2], detergents [3] or polymeric micelles [4,5] with following action of cyclodextrins, as well as cyclodextrins themselves [6]. These approaches are very promising though cyclodextrin itself can affect the proteins [7,8]. Another way is the use of liposomes [9].…”

Section: Introductionmentioning

confidence: 99%

Artificial chaperones based on thermoresponsive polymers recognize the unfolded state of the protein

Semenyuk

Tiainen

Hietala

et al. 2019

International Journal of Biological Macromolecules

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The chaperone-like activity of thermoresponsive polymers based on poly(dimethylaminoethyl methacrylate) (PDMAEMA) was studied on two different proteins, glyceraldehyde-3-phosphate dehydrogenase and chicken egg lysozyme. The polymers do not interact with the folded protein at room temperature but form a complex upon heating to either protein unfolding or polycation phase transition temperature. A PDMAEMA-PEO block copolymer with a dodecyl end-group (d-PDMAEMA-PEO) as well as PDMAEMA-PEO without the dodecyl groups protected the denatured protein against aggregation in contrast to PDMAEMA homopolymer. No effect of the polymers on the enzymatic activity of the client protein was observed at room temperature. The polymers also partially protected the enzyme against inactivation at high temperature. The results provide a platform for creation of artificial chaperones with unfolded protein recognition which is a major feature of natural chaperones. The thermoresponsive polymers can be also used for reversible sedimentation of the folded enzyme.

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Effect of 2‐hydroxypropyl‐β‐cyclodextrin on thermal stability and aggregation of glycogen phosphorylase b from rabbit skeletal muscle

Cited by 17 publications

References 38 publications

A Protein Aggregation Based Test for Screening of the Agents Affecting Thermostability of Proteins

A Protein Aggregation Based Test for Screening of the Agents Affecting Thermostability of Proteins

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

Artificial chaperones based on thermoresponsive polymers recognize the unfolded state of the protein

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