Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2

Moosavi-Movahedi, Ali Akbar; Pirzadeh, Payman; Hashemnia, Sedigheh; Ahmadian, Shahin; Hemmateenejad, Bahram; Amani, Mojtaba; Saboury, Ali Akbar; Ahmad, Faizan; Shamsipur, Mojtaba; Hakimelahi, G. H.; Tsai, Fu-Yuan; Hadi-Alijanvand, Hamid; Yousefi, Reza

doi:10.1016/j.colsurfb.2007.05.018

Cited by 34 publications

(18 citation statements)

References 26 publications

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“…The two states end up quite close to each other. The similar effects of SDS and TFE are noteworthy considering their similar effects in various protein systems, where they both induce β-strand formation at lower concentrations and α-helix formation at higher [17], [18], [19], [20], [21].…”

Section: Resultsmentioning

confidence: 79%

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

et al. 2010

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To obtain insight into the functions of proteins and their specific roles, it is important to establish efficient procedures for exploring the states that encapsulate their conformational space. Global Protein folding State mapping by multivariate NMR (GPS NMR) is a powerful high-throughput method that provides such an overview. GPS NMR exploits the unique ability of NMR to simultaneously record signals from individual hydrogen atoms in complex macromolecular systems and of multivariate analysis to describe spectral variations from these by a few variables for establishment of, and positioning in, protein-folding state maps. The method is fast, sensitive, and robust, and it works without isotope-labelling. The unique capabilities of GPS NMR to identify different folding states and to compare different unfolding processes are demonstrated by mapping of the equilibrium folding space of bovine α-lactalbumin in the presence of the anionic surfactant sodium dodecyl sulfate, SDS, and compare these with other surfactants, acid, denaturants and heat.

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Section: Resultsmentioning

confidence: 79%

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

et al. 2010

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“…Suitable aggregation conditions with submicellar SDS, some at neutral pH, have been identified for other proteins such as S6, 18 Aβ, 19 β 2 -microglobulin, 20 collagen, 59 and lysozyme. 21 Similar types of amphiphile-driven aggregation may occur in vivo. For example, fatty acids such as oleic acid can form higher-order complexes with α-lactalbumin and related proteins with potent anti-cancer properties.…”

Section: Discussionmentioning

confidence: 95%

“…This is particularly pronounced at low pH, where aggregation appears to lead to amorphous precipitates, 18 but also occurs at neutral pH, leading to orderly or fibrillar aggregate structures for proteins as diverse as Aβ, 19 β 2 -microglobulin, 20 S6, 18 and lysozyme. 21 The increased aggregation propensity is undoubtedly related to the ability of SDS to stabilize aggregation-prone structures that represent species at the very early stage of the aggregation process. As such, the mechanism by which surfactants stimulate aggregation may provide important information about aggregation pathways in biological contexts.…”

Section: Introductionmentioning

confidence: 99%

The Role of Decorated SDS Micelles in Sub-CMC Protein Denaturation and Association

Andersen

Oliveira

Larsen

et al. 2009

Journal of Molecular Biology

140

111

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“…However, the AFs disappeared during prolonged incubation. Fibril formation also occurs upon incubation of LYS at pH 9.2 in the presence of SDS (Khan et al., ; Moosavi‐Movahedi et al., ). Based on these findings, it was concluded that both electrostatic and hydrophobic forces are prerequisites for fibril formation, with the former playing a leading role (Khan et al., ).…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

Jansens

Lambrecht

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Conditions including heating mode, time, temperature, pH, moisture and protein concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes, and/or salt influence amyloid fibril (AF) formation as they can affect the accessibility of amino acid sequences prone to aggregate. As some conditions applied on model protein resemble conditions in food processing unit operations, we here hypothesize that food processing can lead to formation of protein AFs with a compact cross β‐sheet structure. This paper reviews conditions and food constituents that affect amyloid fibrillation of egg and cereal proteins. While egg and cereal proteins often coexist in food products, their impact on each other's fibrillation remains unknown. Hen egg ovalbumin and lysozyme form AFs when subjected to moderate heating at acidic pH separately. AFs can also be formed at higher pH, especially in the presence of alcohols or chaotropic/reducing agents. Tryptic wheat gluten digests can form fibrillar structures at neutral pH and maize and rice proteins do so in aqueous ethanol or at acidic pH, respectively.

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Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2

Cited by 34 publications

References 26 publications

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

The Role of Decorated SDS Micelles in Sub-CMC Protein Denaturation and Association

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

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