Dual behavior of sodium dodecyl sulfate as enhancer or suppressor of insulin aggregation and chaperone-like activity of camel αS1-casein

Badraghi, Jalil; Moosavi-Movahedi, Ali Akbar; Saboury, Ali Akbar; Yousefi, Reza; Sharifzadeh, Ahmad; Hong, Jun; Haertlé, Thomas; Niasari-Naslaji, Amir

doi:10.1016/j.ijbiomac.2009.08.008

Cited by 10 publications

(6 citation statements)

References 42 publications

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“…Variation in aggregation-preventing effect has been observed, depending on the polarity of N-terminal region of casein [104], or more generally, on its net charge, and surface hydrophobicity which was demonstrated for camel and bovine caseins [105,106]. In one study involving yeast hexokinase B, the presence of casein and its subsequent removal by cyclodextrin was effective in protecting the enzyme from aggregation and denaturation, presumably by a "chaperone-assisted refolding" mechanism [107].…”

Section: Chaperone-like Substancesmentioning

confidence: 99%

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Ebrahim‐Habibi

Morshedi

Rezaei‐Ghaleh

et al. 2010

JICS

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Protein aggregates, whether amorphous or structured (amyloid), have attracted much attention in recent years and despite extensive efforts, the mechanism of their formation is poorly understood. While "natural" aggregation (polymerization) of monomers could improve the biological function of some proteins, it is usually the darker side of this phenomenon which is discussed in many studies: deleterious aggregation that could lead to loss of biological activity under in vitro conditions or cause misfolding diseases. In this review, protein aggregation has been overviewed, starting from some general concepts involved in its formation, followed by mentioning studies aimed at elucidation of its kinetics and mechanism, or characterization of intermediates that would be aggregation-prone, and finally, reporting some of the studies related to the design of methods that would control the process. Similarly, amyloid aggregates have been defined, and current methods used in their characterization have been briefly described, with an emphasis on in silico studies. Finally, identification and design of such molecules which may be effective in control of this process is discussed.

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Section: Chaperone-like Substancesmentioning

confidence: 99%

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Ebrahim‐Habibi

Morshedi

Rezaei‐Ghaleh

et al. 2010

JICS

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“…The reaction of WRK with a carboxylate is outlined in Scheme 1 [29]. Recent studies have shown that ␤-casein acts as a molecular chaperone when it interacts with proteins that have negative charge on their surface, including insulin [20,30] and alcohol dehydrogenase [17,[31][32][33]. The presence of negative charge on ␤-casein surface, which results in electrostatic and hydrophobic factors to act in the same direction, promotes ␤-casein molecular chaperone property.…”

Section: Introductionmentioning

confidence: 99%

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Moosavi-Movahedi

Rajabzadeh

Amani

et al. 2011

International Journal of Biological Macromolecules

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“…This leads to the proposal that promoting the formation of helical structures in pro teins is likely to inhibit their aggregation as it will enhance the population of species that undergo intrachain interac tions and, hence, will reduce the propensity for inter polypeptide association [13,16]. This strategy has been proposed mainly in the context of those proteins that undergo amyloid fibril formation that is associated with neurodegenerative diseases [14,16,17]. However, it has not been discussed whether this approach can be applied in the case of industrially important proteins, which are not only required to be protected against aggregation but also need to remain functionally active in the presence of aggregation inhibitors.…”

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confidence: 99%

Inhibitory effect of post-micellar SDS concentration on thermal aggregation and activity of papain

Qadeer

Zaman

Khan

2014

Biochemistry Moscow

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Papain, a cysteine protease isolated from the latex of Carica papaya, is known to undergo irreversible thermal unfolding. In this study, we found that thermal unfolding of papain is accompanied by a simultaneous self-assembly process where this protein is observed to aggregate above 50°C. The extent of aggregation increased with increasing protein concentration from 3-40 µM. The aggregation was confirmed by enhanced turbidity, light scattering intensity, 1-anilino-8-naphthalene sulfonate (ANS) fluorescence intensity and by transmission electron microscopy. Furthermore, we noted that post-micellar concentration of sodium dodecyl sulfate (SDS) remarkably suppresses the thermal aggregation of papain. Far-UV circular dichroism studies revealed that SDS significantly enhances α-helical content of the protein and also tends to prevent its unfolding, and thus inhibits aggregation. Additionally, papain showed maximal activity at 65°C in neutral buffer. However, in the presence of 6 mM SDS (above its critical micellar concentration), the enzyme lost activity by about 10-fold. Thus, promoting the helical propensity of the protein does not appear to be a suitable strategy to overcome the aggregation related problems of industrially important proteins such as papain, which are not only required to be protected against aggregation but also need to remain functionally active in the presence of aggregation inhibitors.

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Dual behavior of sodium dodecyl sulfate as enhancer or suppressor of insulin aggregation and chaperone-like activity of camel αS1-casein

Cited by 10 publications

References 42 publications

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Inhibitory effect of post-micellar SDS concentration on thermal aggregation and activity of papain

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