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Understanding protein adsorption phenomena at solid surfaces

TLDR
In this review recent achievements and new perspectives on protein adsorption processes are comprehensively discussed and the main focus is put on commonly postulated mechanistic aspects and their translation into mathematical concepts and model descriptions.
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This article is published in Advances in Colloid and Interface Science.The article was published on 2011-02-17 and is currently open access. It has received 1328 citations till now.

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The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions

TL;DR: This review will tackle the current understanding of protein aggregation in the framework of foods, which is possibly one of the broadest contexts, yet is of tremendous daily relevance.
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Nanoparticle–Cell Interactions: Molecular Structure of the Protein Corona and Cellular Outcomes

TL;DR: The observation that similar NPs with identical protein corona compositions bind to different cellular receptors suggested that a difference in the structure of the adsorbed protein may be responsible for the differences in cellular binding of the protein–NP complexes.
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Enhanced Activity of Enzymes Encapsulated in Hydrophilic Metal-Organic Frameworks.

TL;DR: It is shown that enzymes encapsulated within hydrophilic MAF-7 or Zif-90 retain enzymatic activity upon encapsulation and when exposed to high temperatures, denaturing or proteolytic agents, and organic solvents, whereas hydrophobic ZIF-8 affords inactive catalase and negligible protection to urease.
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Proteins, platelets, and blood coagulation at biomaterial interfaces.

TL;DR: Appropriate use of surface texturing and chemical patterning methodologies allow for reduction of both blood coagulation and platelet adhesion, and new methods of surface interrogation at high resolution allow for measurement of the relevant biological factors.
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Intermolecular and surface forces

TL;DR: The forces between atoms and molecules are discussed in detail in this article, including the van der Waals forces between surfaces, and the forces between particles and surfaces, as well as their interactions with other forces.
Journal ArticleDOI

Imaging intracellular fluorescent proteins at nanometer resolution.

TL;DR: This work introduced a method for optically imaging intracellular proteins at nanometer spatial resolution and used this method to image specific target proteins in thin sections of lysosomes and mitochondria and in fixed whole cells to image retroviral protein Gag at the plasma membrane.
Journal ArticleDOI

Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM).

TL;DR: A high-resolution fluorescence microscopy method based on high-accuracy localization of photoswitchable fluorophores that can, in principle, reach molecular-scale resolution is developed.
Journal ArticleDOI

Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy

TL;DR: A new type of scanning fluorescence microscope capable of resolving 35 nm in the far field is proposed, overcome the diffraction resolution limit by employing stimulated emission to inhibit the fluorescence process in the outer regions of the excitation point-spread function.
Book

Proteins: Structures and Molecular Properties

TL;DR: This paper discusses the physical properties of polypeptides, the structure of which has been determined Crystallographically to High Resolution and its role in the biosynthesis of Proteins.
Related Papers (5)
Frequently Asked Questions (6)
Q1. What is the pathological component of Parkinson’s disease?

Inversely to protein aggregation in solution, the direct growth of aggregates on the surface can also be observed using the protein α-Synuclein which is the pathological component of Parkinson’s disease. 

The present dissertation aims to advance the understanding of protein adsorption and to systematically unravel the underlying molecular mechanism. One of the comprehensively studied adsorption phenomena is cooperativity which refers to the effect that the adsorption of proteins is enhanced by the presence of pre-adsorbed proteins. The significance of this work results from the successful combination of substantial experimental investigations with efficient theoretical methods giving access to a clear and illustrative view on some exciting adsorption phenomena. Instead, a macroscopic model description is suggested that simply assumes the overlap of two parallel adsorption pathways, one for the adsorption at isolated surface positions and one for the adsorption near other surface-bound proteins. Further, a microscopic treatment of the mechanism behind cooperativity is realized through Monte-Carlo simulations which reproduce the experimental data accurately and thereby confirm the suggestion that approaching proteins can be tracked to favorable binding sites near other pre-adsorbed proteins. 

The most important method used to study the corresponding model systems was FRET imaging. Evaluating the effects of the discussed mechanism on the biological activity and cytotoxicity of the proteins and designing interfaces that allow for a certain control over aggregation processes will be important topics for future research. As a consequence, the deposition of protein clusters on the surface can be suppressed by a dense protein monolayer provided that it displays a low surface mobility of adsorbed proteins. This suggests that the growth of the fibrils starts at the initially determined positions which in the end remain the surface anchoring sites and proceeds in a certain direction not necessarily along the surface. 

The significance of this work results from the successful combination of substantial experimental investigations with efficient theoretical methods giving access to a clear and illustrative view on some exciting adsorption phenomena. 

Entgegen einer weit verbreitenden Ansicht kann gezeigt werden, dass Kooperativität nicht zwangsläufig mit der Aggregation von Proteinen auf der Oberfläche einhergeht. 

Whereas the on-surface growth mechanism is the typically proposed one when protein aggregates are detected on a surface, the discovery that protein aggregates can also come from the solution and spread on the surface opens a completely new perspective on this topic.