On the complexation of whey proteins

Delboni, Lariani Aparecida; Silva, Fernando Luís Barroso da

doi:10.1016/j.foodhyd.2015.11.010

Cited by 41 publications

(132 citation statements)

References 82 publications

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“…This means that coacervation occurs for a specific balance of attractive and repulsive interactions and not only as a consequence of the interactions between 2 oppositely charged molecules. The calculated free energy of the interaction between LF and β-LG indicates that the pH window of maximal interaction is 6.5-8.0 while coacervation range is observed at lower pH [62]. Interestingly the optimal pH of coacervation depends on β-LG variant ( Fig.…”

Section: Accepted Manuscriptmentioning

confidence: 92%

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Heteroprotein complex coacervation: A generic process

Croguennec

Tavares

Bouhallab

2017

Advances in Colloid and Interface Science

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Proteins exhibit a rich diversity of functional, physico-chemical and biodegradable properties which makes them appealing for various applications in the food and non-food sectors. Such properties are attributed to their ability to interact and assemble into a diversity of supramolecular structures. The present review addresses the updated research progress in the recent field of complex coacervation made from mixtures of oppositely charged proteins (i.e. heteroprotein systems). First, we describe briefly the main proteins used for heteroprotein coacervation. Then, through some selected examples, we illustrate the particularity and specificity of each heteroprotein system and the requirements that drive optimal assembly into coacervates. Finally, possible and promising applications of heteroprotein coacervates are mentioned.

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Section: Accepted Manuscriptmentioning

confidence: 92%

“…The observed difference in the range of ionic strength for coacervation could result either from different protein concentrations used as predicted by simulation [62] and/or from the quality of used protein samples, i.e. β-LG isoforms, iron saturation degree of LF, protein denaturation rate.…”

Section: Effect Of Ionic Strengthmentioning

confidence: 99%

Heteroprotein complex coacervation: A generic process

Croguennec

Tavares

Bouhallab

2017

Advances in Colloid and Interface Science

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“…Following a coarse-grained (CG) description of the macromolecular system (Noid 2013) in implicit solvent and a phenomenological physical chemical approach, the FPTS for proteins was proposed (Teixeira et al 2010) successfully reducing the computation time and also efficiently boosting sampling for applications in protein complexation studies (e.g., Teixeira et al (2010), Persson et al (2010), Kurut et al (2015), Delboni and Barroso da Silva (2016), and Barroso da Silva et al (2016)). This is clearly the main differential of this titration method that forward biomolecular applications on the large-scale scenario for protein-protein, protein-RNA/DNA, protein-polyelectrolyte and proteinnanoparticle interactions.…”

Section: Titration Schemes Based On the Monte Carlo Methodsmentioning

confidence: 99%

“…The CpH MC schemes in implicit solvents discussed above meet well all these requirements. They have been intensively and successfully applied in several biomolecular systems: (a) protein-protein interactions Jönsson 2003, 2005;Jönsson et al 2007;Persson et al 2010;Kurut et al 2012Kurut et al , 2015Delboni and Barroso da Silva 2016;Barroso da Silva et al 2016), (b) protein-polyelectrolyte interactions (Barroso da Jönsson et al 2007; Barroso da Silva and Jönsson 2009;Barroso da Silva 2013;Srivastava et al 2017), (c) protein-peptide interactions (André et al 2004;Jönsson et al 2007), (d) protein-surface interactions (Nylander et al 2017;Hyltegren and Skepö 2017), and (e) protein-nanoparticle interactions (Barroso da Silva et al 2014;Carnal et al 2015). There is also ongoing work on protein-RNA interactions at our laboratory together with Profs.…”

Section: Simplified Models Applications In Biomolecular Systemsmentioning

confidence: 99%

“…Studies have also reported pH-dependent ATPase activity (Jin et al 2017). Other common examples of processes controlled by pH include protein/RNA stability and folding, (Stigter and Dill 1990;Garcia-Moreno 1995;Harano and Kinoshita 2006;Tang et al 2007;Thaplyal and Bevilacqua 2014) regulation through conformational switches, (Lizatović et al 2016) amyloid formation, (Enciso et al 2013) proteinpolyelectrolyte association, (Barroso da Silva and Jönsson 2009;Stoll 2014) protein-nanoparticle interactions (Chen et al 2011;Barroso da Silva et al 2014) protein-protein complexation (Sheinerman et al 2000;Lund and Jönsson 2013;Delboni and Barroso da Silva 2016) and protein-RNA interactions (Ye et al 2003;Koukiekolo et al 2007; Barroso da Silva et al 2017c). All these biomolecular systems are of importance too in many technological systems in food, brewing, pharma, bioseparations, and biomaterials in general (Chen et al 2011;Steiner et al 2011;Egan et al 2014; Barroso da Wagoner et al 2016).…”

Section: Introductionmentioning

confidence: 99%

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Development of constant-pH simulation methods in implicit solvent and applications in biomolecular systems

daSilva

Dias

2017

Biophys Rev

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pH is a critical parameter for biological and technological systems directly related with electrical charges. It can give rise to peculiar electrostatic phenomena, which also makes them more challenging. Due to the quantum nature of the process, involving the forming and breaking of chemical bonds, quantum methods should ideally by employed. Nevertheless, due to the very large number of ionizable sites, different macromolecular conformations, salt conditions, and all other charged species, the CPU time cost simply becomes prohibitive for computer simulations, making this a quite complex problem. Simplified methods based on Monte Carlo sampling have been devised and will be reviewed here, highlighting the updated state-ofthe-art of this field, advantages, and limitations of different theoretical protocols for biomolecular systems (proteins and nucleic acids). Following a historical perspective, the discussion will be associated with the applications to protein interactions with other proteins, polyelectrolytes, and nanoparticles.

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A revised order of subunits in mammalian septin complexes

Mendonça¹,

Macêdo

Guimarães³

et al. 2019

Cytoskeleton

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Septins are GTP binding proteins considered to be novel components of the cytoskeleton. They polymerize into filaments based on hexameric or octameric core particles in which two copies of either three or four different septins, respectively, assemble into a specific sequence. Viable combinations of the 13 human septins are believed to obey substitution rules in which the different septins involved must come from distinct subgroups. The hexameric assembly, for example, has been reported to be SEPT7–SEPT6–SEPT2–SEPT2–SEPT6–SEPT7. Here, we have replaced SEPT2 by SEPT5 according to the substitution rules and used transmission electron microscopy to demonstrate that the resulting recombinant complex assembles into hexameric particles which are inverted with respect that predicted previously. MBP‐SEPT5 constructs and immunostaining show that SEPT5 occupies the terminal positions of the hexamer. We further show that this is also true for the assembly including SEPT2, in direct contradiction with that reported previously. Consequently, both complexes expose an NC interface, as reported for yeast, which we show to be more susceptible to high salt concentrations. The correct assembly for the canonical combination of septins 2‐6‐7 is therefore established to be SEPT2–SEPT6–SEPT7–SEPT7–SEPT6–SEPT2, implying the need for revision of the mechanisms involved in filament assembly.

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On the complexation of whey proteins

Cited by 41 publications

References 82 publications

Heteroprotein complex coacervation: A generic process

Heteroprotein complex coacervation: A generic process

Development of constant-pH simulation methods in implicit solvent and applications in biomolecular systems

A revised order of subunits in mammalian septin complexes

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