Amyloid fibrillation of hen egg-white lysozyme is inhibited by TCEP

Wang, Steven S.‐S.; Liu, Kuan-Nan; Yu-qi, LU

doi:10.1016/j.bbrc.2009.02.103

Cited by 30 publications

(18 citation statements)

References 27 publications

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“…7,8 Given the dramatic impact of protein oligomers on the development of severe diseases, and allowing for the perceived importance of lipid matrices in polypeptide self-assembly, accurate detection and characterization of lipid-assisted protein aggregation are of utmost significance, since timely identification of oligomers may help to prevent their conversion into pathogenic species. To date, the vast majority of experimental techniques including circular dichroism, 9 atomic force and electron microscopy, 10,11 electron paramagnetic resonance, 12 etc. has been employed to clarify the role of lipid bilayer in protein aggregation.…”

Section: Introductionmentioning

confidence: 99%

Förster Resonance Energy Transfer Evidence for Lysozyme Oligomerization in Lipid Environment

et al. 2010

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Intermolecular time-resolved and single-molecule Förster resonance energy transfer (FRET) have been applied to detect quantitatively the aggregation of polycationic protein lysozyme (Lz) in the presence of lipid vesicles composed of phosphatidylcholine (PC) and its mixture with 5, 10, 20, or 40 mol % of phosphatidylglycerol (PG) (PG5, PG10, PG20, or PG40, respectively). Upon binding to PC, PG5, or PG10 model membranes, Lz was found to retain its native monomeric conformation, while increasing content of anionic lipid up to 20 or 40 mol % resulted in the formation of Lz aggregates. The structural parameters of protein self-association (the degree of oligomerization, the distance between the monomers in protein assembly, and the fraction of donors present in oligomers) have been derived. The crucial role of the factors such as lateral density of the adsorbed protein and electrostatic and hydrophobic Lz–lipid interactions in controlling the protein self-association behavior has been proposed.

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Section: Introductionmentioning

confidence: 99%

Förster Resonance Energy Transfer Evidence for Lysozyme Oligomerization in Lipid Environment

et al. 2010

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“…31 Furthermore, our laboratory has recently demonstrated that hen lysozyme's propensity for fibrillation at low pH and elevated temperature may attenuate significantly in the presence of free thiol/sulfhydryl groups. 68 The results reported here also implicate a potential use of reducing agents for inhibition of amyloid fibrillation.…”

Section: Discussionmentioning

confidence: 70%

“…This finding is in line with those revealed from the researches using other reducing agents (e.g., TCEP and DTT) and/or proteins (e.g., hen eggwhite lysozyme). 68,69 A large number of studies have been directed toward seeking or developing potential compounds/molecules to inhibit or prevent amyloid fibrillation and several compounds have been found to retard the formation of fibrils both in vitro and in vivo. 27,28 Similar to other reducing agents such as DTT and cysteine, GSH has been employed by other investigators to disrupt intermolecular disulfide bridges of proteins, protein fragments, and disulfidecontaining surfactant in denaturing conditions.…”

Section: Discussionmentioning

confidence: 99%

Fibril Formation of Bovine α-Lactalbumin Is Inhibited by Glutathione

et al. 2011

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The current research is aimed at exploring the inhibitory effect of glutathione on fibril formation of an important four disulfide bond-containing whey protein, α-lactalbumin. Through numerous spectroscopic techniques and transmission electron microscopy, we found that the inhibition of amyloid formation of α-lactalbumin was dependent on the glutathione concentration and fibrillation was significantly attenuated in the presence of 5 mM glutathione. Moreover, the data from the measurements using 4,4′-dithiodipyridine reagent revealed that the treatment of α-lactalbumin with glutathione led to the exposure of sulfhydryl groups. Also, the observed inhibition of α-lactalbumin by glutathione was correlated with the reduction of disulfide bridges of protein. The results presented here suggest that the addition of food compatible reducing agent/dietary supplement such as glutathione would be useful for preventing the formation of milk protein fibrillar aggregates. The presence of these resulting aggregates can then, in turn, be used to modulate the key properties of food products such as protein beverage and yogurt.

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“…During amyloid formation, the disulfide bonds in lysozyme become more accessible to the solvent [19] and free thiols may be produced due to disulfide breakage, particularly in the presence of thiol-reacting reagents or reducing compounds [44][45][46]. In another experiment, the production of free thiols in the process of lysozyme fibrillation was confirmed by the Ellman method [47].…”

Section: Discussionmentioning

confidence: 76%