Protein Unfolding and Aggregation near a Hydrophobic Interface

March, David; Bianco, Valentino; Franzese, Giancarlo

doi:10.3390/polym13010156

Cited by 32 publications

(36 citation statements)

References 55 publications

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“…The thin layer of water that directly hydrates the membrane, commonly referred to as biological water, , has been proven to actively participate in the biological functioning of DNA . Moreover, biological water is inherently connected with the process of protein folding, aggregation, , and stabilization of the structure even in extreme thermodynamic conditions . Numerous experiments aimed at understanding the properties of biological water, using nuclear magnetic resonance, X-ray and neutron scattering, , infrared spectroscopy, sum frequency generation, , and molecular dynamics simulations, − among others, showed that water molecules form a network structure, being bound by hydrogen bonds and weak van der Waals interactions around the polar head group, the so-called clathrate hydration structure .…”

Section: Introductionmentioning

confidence: 99%

Hydration Layer of Only a Few Molecules Controls Lipid Mobility in Biomimetic Membranes

et al. 2021

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Self-assembly of biomembranes results from the intricate interactions between water and the lipids’ hydrophilic head groups. Therefore, the lipid–water interplay strongly contributes to modulating membrane architecture, lipid diffusion, and chemical activity. Here, we introduce a new method of obtaining dehydrated, phase-separated, supported lipid bilayers (SLBs) solely by controlling the decrease of their environment’s relative humidity. This facilitates the study of the structure and dynamics of SLBs over a wide range of hydration states. We show that the lipid domain structure of phase-separated SLBs is largely insensitive to the presence of the hydration layer. In stark contrast, lipid mobility is drastically affected by dehydration, showing a 6-fold decrease in lateral diffusion. At the same time, the diffusion activation energy increases approximately 2-fold for the dehydrated membrane. The obtained results, correlated with the hydration structure of a lipid molecule, revealed that about six to seven water molecules directly hydrating the phosphocholine moiety play a pivotal role in modulating lipid diffusion. These findings could provide deeper insights into the fundamental reactions where local dehydration occurs, for instance during cell–cell fusion, and help us better understand the survivability of anhydrobiotic organisms. Finally, the strong dependence of lipid mobility on the number of hydrating water molecules opens up an application potential for SLBs as very precise, nanoscale hydration sensors.

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Section: Introductionmentioning

confidence: 99%

Hydration Layer of Only a Few Molecules Controls Lipid Mobility in Biomimetic Membranes

et al. 2021

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“…In aqueous media, proteins undergo many physicochemical changes such as conformational alterations, denaturation, folding/unfolding processes, and ligand exchange [1][2][3][4][5][6]. These phenomena can be invoked by variations in the temperature and/or the pH of a solution.…”

Section: Introductionmentioning

confidence: 99%

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

et al. 2021

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The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)4]−) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)4]− for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)4]− ions (logK(ITC)1 = 7.09 ± 0.10; ΔG(ITC)1 = −9.67 ± 0.14 kcal mol−1; ΔH(ITC)1 = −3.14 ± 0.12 kcal mol−1; TΔS(ITC)1 = −6.53 kcal mol−1), whereas the second site is localized in the subdomain III A and binds five ions (logK(ITC)2 = 5.39 ± 0.06; ΔG(ITC)2 = −7.35 ± 0.09 kcal mol−1; ΔH(ITC)2 = 4.00 ± 0.14 kcal mol−1; TΔS(ITC)2 = 11.3 kcal mol−1). The formation of the {[B(Ph)4]−}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.

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“…If a protein has a hydrophobic side chain, it may adsorb onto lipid bilayer membranes (Arbuzova et al, 1998). Protein adsorption and denaturation at interfaces such as water/oil or water/air is a widely recognized phenomenon (March et al, 2021).…”

Section: Macromolecular Confinement and Adsorptionmentioning

confidence: 99%

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Bao

Ertbjerg

Estévez

et al. 2021

Comp Rev Food Sci Food Safe

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Over the recent decades,protein oxidation in muscle foods has gained increasing research interests as it is known that protein oxidation can affect eating quality and nutritional value of meat and aquatic products. Protein oxidation occurs during freezing/thawing and frozen storage of muscle foods, leading to irreversible physicochemical changes and impaired quality traits. Controlling oxidative damage to muscle foods during such technological processes requires a deeper understanding of the mechanisms of freezing-induced protein oxidation. This review focus on key physicochemical factors in freezing/thawing and frozen storage of muscle foods, such as formation of ice crystals, freeze concentrating and macromolecular crowding effect, instability of proteins at the icewater interface, freezer burn, lipid oxidation, and so on. Possible relationships between these physicochemical factors and protein oxidation are thoroughly discussed. In addition, the occurrence of protein oxidation, the impact on eating quality and nutrition, and controlling methods are also briefly reviewed. This review will shed light on the complicated mechanism of protein oxidation in frozen muscle foods.

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Protein Unfolding and Aggregation near a Hydrophobic Interface

Cited by 32 publications

References 55 publications

Hydration Layer of Only a Few Molecules Controls Lipid Mobility in Biomimetic Membranes

Hydration Layer of Only a Few Molecules Controls Lipid Mobility in Biomimetic Membranes

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

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