Computer simulation of proteins: adsorption, gelation and self-association

Euston, Stephen R.

doi:10.1016/j.cocis.2004.09.005

Cited by 50 publications

(41 citation statements)

References 53 publications

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“…An increasingly important access to molecular-scale studies of protein adsorption events has been opened by computational methods [263][264][265][266]. The adsorption of one or several proteins to a selected surface is simulated with differing degrees of exactness based on physical laws.…”

Section: Computational Approachesmentioning

confidence: 99%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,386

1,239

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Protein adsorption at solid surfaces plays a key role in many natural processes and has therefore promoted a widespread interest in many research areas. Despite considerable progress in this field there are still widely differing and even contradictive opinions on how to explain the frequently observed phenomena such as structural rearrangements, cooperative adsorption, overshooting adsorption kinetics, or protein aggregation. In this review recent achievements and new perspectives on protein adsorption processes are comprehensively discussed. The main focus is put on commonly postulated mechanistic aspects and their translation into mathematical concepts and model descriptions. Relevant experimental and computational strategies to practically approach the field of protein adsorption mechanisms and their impact on current successes are outlined.

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Section: Computational Approachesmentioning

confidence: 99%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,386

1,239

View full text Add to dashboard Cite

show abstract

“…Previous investigations of proteins at interfaces have shown that proteins will often adsorb and denature at an interface to form a film. [38,39] These studies have shown that the rate of film formation for most proteins is slow, taking from minutes to hours, since several processes have to take place in a defined order: i) protein adsorption, ii) protein unfolding, and iii) protein refolding and assembly. [39] The adsorption is entropic in origin and is largely driven by amino acid residues displacing water from the interfacial region.…”

mentioning

confidence: 98%

“…[39] The adsorption is entropic in origin and is largely driven by amino acid residues displacing water from the interfacial region. [38] The mechanism of silk-protein assembly is thought to be similar to the adsorption of other proteins at surfaces (Fig. 1).…”

mentioning

confidence: 99%

Engineered Microcapsules Fabricated from Reconstituted Spider Silk

et al. 2007

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In applications such as flavor encapsulation, drug delivery, and biomedical devices, microencapsulation is developing into an increasingly effective method for the protection and delivery of active ingredients. Herein, we show that spider-silk proteins are well-suited for producing responsive microcapsules with high mechanical stability. Emulsion interfaces are harnessed to induce the controlled self-assembly of these proteins into predominantly b-sheet configurations, resulting in a mechanically stable thin polymer shell. Capsules transferred into a continuous phase can readily encapsulate large molecules, while allowing small molecules to permeate freely. The capsules demonstrate good chemical stability, which is attributed to the b-sheet-rich structure of the self-assembled spider-silk proteins. These microcapsules represent a new class of biomimetic materials, exhibiting functionalities that can be further modified and controlled on the molecular level.

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“…The interaction of biological macromolecules, in particular proteins, with a foreign surface is a closely related field that play an important role in a wide range of biological processes (such as cell aggregation and interaction of ligands with membrane receptors) and is not easily amenable to theory owing to the structural details at the atomistic level and the denaturation process these molecules can undergo upon adsorption. In recent years, computer simulations have added significant new insights, complementing both theory and experiments (Noinville et al 1995;Euston 2004;Ganazzoli & Raffaini 2005). The atomistic computer simulations are the only techniques that can deal with this task, providing a realistic description of the adsorption process, although the size and the complexity of the problem are often discouraging.…”

Section: Introductionmentioning

confidence: 99%

“…The simulations were carried out by using a two-step strategy, with direct energy minimizations of selected HSA subdomains close to the chrysotile surface, using an effective dielectric medium with a distancedependent dielectric constant to account for the dipolar interactions (Raffaini & Ganazzoli 2003, 2004. Extensive MD runs of the previously minimized subdomains follow with subsequent energy minimization of the instantaneous snapshots.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of human serum albumin on the chrysotile surface: a molecular dynamics and spectroscopic investigation

Artali

Prà

Foresti

et al. 2007

J. R. Soc. Interface.

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The human serum albumin (HSA) secondary structure modifications induced by the chrysotile surface have been investigated via computational molecular dynamics (MD) and experimental infrared spectroscopy (FTIR) on synthetic chrysotile nanocrystals coated with different amount of HSA. MD simulations, conducted by placing various albumin subdomains close to the fixed chrysotile surface, show an initial adsorption phase, accompanied by local rearrangements of the albumin motifs in contact with the chrysotile layer. Next, large-scale rearrangements follow with consequent secondary structure modifications.Gaussian curve fitting of the FTIR spectra obtained for HSA-coated synthetic chrysotile nanocrystals has allowed the quantification of HSA structural modifications as a function of the amount of protein adsorbed. The experimental results support the atomistic computer simulations providing a realistic description of the adsorption of plasma proteins onto chrysotile and unravelling a key step in the understanding of asbestos toxicity.

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Computer simulation of proteins: adsorption, gelation and self-association

Cited by 50 publications

References 53 publications

Understanding protein adsorption phenomena at solid surfaces

Understanding protein adsorption phenomena at solid surfaces

Engineered Microcapsules Fabricated from Reconstituted Spider Silk

Adsorption of human serum albumin on the chrysotile surface: a molecular dynamics and spectroscopic investigation

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