Protein Adsorption and Conformational Changes

Assfalg, Michael

doi:10.3390/molecules26237079

Cited by 7 publications

(5 citation statements)

References 17 publications

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“…21,22 However, our comprehension of these mechanisms must still be completed. 23 Also, the effect of adsorption on a flat surface can be highly diverse when comparing structured regions with IDRs of the same protein. 24 Hence, understanding the impact of the interface on the protein's conformation is crucial in determining nanomaterial interactions with biological environments.…”

Section: Introductionmentioning

confidence: 99%

Intrinsically disordered protein’s coil-to-globule transition and adsorption onto a hydrophobic surface under different conditions

Fauli

Bianco²,

Franzese

2023

Preprint

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Intrinsically disordered proteins (IDPs) and proteins with intrinsically disordered regions (IDRs) can modulate cellular responses to environmental conditions by undergoing coil-to-globule transitions and phase separation. However, the molecular mechanisms of these phenomena still need to be fully understood. Here, we use Monte Carlo calculations of a model incorporating water's effects on the system's free energy to investigate how an IDP responds to a hydrophobic surface under different conditions. We show that a slit pore confinement without top-down symmetry enhances the unfolding and adsorption of the IDP in both random coil and globular states. Moreover, we demonstrate that the hydration water modulates this behavior depending on the thermodynamic parameters. Our findings provide insights into how IDPs and IDRs can sense and adjust to external stimuli such as nanointerfaces or stresses.

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Section: Introductionmentioning

confidence: 99%

Intrinsically disordered protein’s coil-to-globule transition and adsorption onto a hydrophobic surface under different conditions

Fauli

Bianco²,

Franzese

2023

Preprint

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“…For example, when nanoparticles come into contact with the bloodstream, they form a corona of multiple layers of proteins and biomolecules. This gives the nanocomplex a new biological identity. , It is generally accepted that, upon adsorption, proteins can alter their structure, − which can have significant consequences like an inflammatory response or fibril formation. , However, our comprehension of these mechanisms must still be completed . Also, the effect of adsorption on a flat surface can be highly diverse when comparing structured regions with IDRs of the same protein .…”

Section: Introductionmentioning

confidence: 99%

“… 22 , 23 However, our comprehension of these mechanisms must still be completed. 24 Also, the effect of adsorption on a flat surface can be highly diverse when comparing structured regions with IDRs of the same protein. 25 Hence, understanding the impact of the interface on the protein’s conformation is crucial in determining nanomaterial interactions with biological environments.…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic Homopolymer’s Coil–Globule Transition and Adsorption onto a Hydrophobic Surface under Different Conditions

Durà

Bianco²,

Franzese

2023

J. Phys. Chem. B

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Unstructured proteins can modulate cellular responses to environmental conditions by undergoing coil−globule transitions and phase separation. However, the molecular mechanisms of these phenomena still need to be fully understood. Here, we use Monte Carlo calculations of a coarse-grained model incorporating water's effects on the system's free energy. Following previous studies, we modeled an unstructured protein as a polymer chain. Because we are interested in investigating how it responds to thermodynamic changes near a hydrophobic surface under different conditions, we chose an entirely hydrophobic sequence to maximize the interaction with the interface. We show that a slit pore confinement without top-down symmetry enhances the unfolding and adsorption of the chain in both random coil and globular states. Moreover, we demonstrate that the hydration water modulates this behavior depending on the thermodynamic parameters. Our findings provide insights into how homopolymers and possibly unstructured proteins can sense and adjust to external stimuli such as nanointerfaces or stresses.

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“…The adsorption of proteins at interfaces is a fundamental step in many natural, biomimetic and applied processes. [1] In the last three decades, this phenomenon has been investigated at the gas/liquid, [2,3] solid/liquid [4][5][6][7] or the non-polarized liquid/liquid interfaces, [8][9][10][11][12] and also at the polarized liquid/liquid interfaces, i. e., the interfaces between two immiscible electrolyte solutions (ITIES). [13][14][15][16][17][18][19][20] The latter system has allowed to investigate the effects of the interfacial potential difference on the adsorption behavior of proteins such as bovine serum albumin, [13,14] glucose oxidase, [15] haemoglobin, [16] lysozyme, [17,18] or myoglobin, [20] as well as the effects of the adsorbed layer on the ion transfer kinetics.…”

Section: Introductionmentioning

confidence: 99%

“…The adsorption of proteins at interfaces is a fundamental step in many natural, biomimetic and applied processes [1] . In the last three decades, this phenomenon has been investigated at the gas/liquid, [2,3] solid/liquid [4–7] or the non‐polarized liquid/liquid interfaces, [8–12] and also at the polarized liquid/liquid interfaces, i. e., the interfaces between two immiscible electrolyte solutions (ITIES) [13–20] .…”

Section: Introductionmentioning

confidence: 99%

Bovine Serum Albumin Adsorption at a Polarized Water/1,2‐Dichloroethane Interface with No Effect on the Ion Transfer Kinetics

2022

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Adsorption of bovine serum albumin (BSA) at a polarized water/1,2‐dichloroethane (DCE) interface is examined by measuring the dynamic interfacial tension γ at various cell potentials E, BSA concentrations and pH of the aqueous phase (w). An addition of BSA to the phase (w) results in an appreciable decay ofγ with time in the whole potential range available, which follows an induction period at the very beginning of the γ transient. An analysis of the effect of the BSA concentration on the γ transients enables to establish the adsorption isotherm, and to evaluate both the maximum surface excess concentration of BSA and the standard Gibbs energy of adsorption. An increase of the potential E results in an acceleration of the adsorption, and an increase of the surface excess concentration of the positively charged BSA at pH 2, while the latter effect is absent when BSA is charged negatively at pH 7.3. It is shown that the adsorbed BSA has a negligible effect on both the interfacial capacitance of the polarized water/DCE interface and the rate constant of the interfacial transfer of the tetraethylammonium (TEA+) or Cs+ ion measured at the corresponding standard ion transfer potential.

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Protein Adsorption and Conformational Changes

Abstract: Protein adsorption onto surfaces of diverse materials of both natural and artificial origin is of utmost relevance in many areas of research and technology: medicine, pharmaceutical sciences, analytical sciences, biotechnology, nanotechnology, and cell biology, among others [...]

Cited by 7 publications

References 17 publications

Intrinsically disordered protein’s coil-to-globule transition and adsorption onto a hydrophobic surface under different conditions

Intrinsically disordered protein’s coil-to-globule transition and adsorption onto a hydrophobic surface under different conditions

Hydrophobic Homopolymer’s Coil–Globule Transition and Adsorption onto a Hydrophobic Surface under Different Conditions

Bovine Serum Albumin Adsorption at a Polarized Water/1,2‐Dichloroethane Interface with No Effect on the Ion Transfer Kinetics

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