SFG analysis of surface bound proteins: a route towards structure determination

Weidner, Tobias; Castner, David G.

doi:10.1039/c3cp50880c

Cited by 79 publications

(99 citation statements)

References 100 publications

(194 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In general, a higher protein coverage is seen for hydrophobic surfaces, due to the higher entropy gain of dehydration 19 . However, when electrostatic effects and conformational changes are dominant, significant adsorption may also be observed for hydrophilic surfaces 20,21 .…”

Section: Introductionmentioning

confidence: 99%

Using Neutron Reflectometry to Discern the Structure of Fibrinogen Adsorption at the Stainless Steel/Aqueous Interface

et al. 2016

View full text Add to dashboard Cite

Neutron reflectometry has been successfully used to study adsorption on a stainless steel surface by means of depositing a thin steel film on silicon. The film was characterized using XPS (X-ray photoelectron spectroscopy), TOF-SIMS (time-of-flight secondary ion mass spectrometry) and GIXRD (grazing incidence X-ray diffraction), demonstrating the retention both of austenitic phase and of the required composition for 316L stainless steel. The adsorption of fibrinogen from a physiologically-relevant solution onto the steel surface was studied using neutron reflectometry and QCM (quartz crystal microbalance) and compared to that on a deposited chromium oxide surface. It was found that the protein forms an irreversibly-bound layer at low concentrations, with maximum protein concentration a distance of around 20 Å from the surface. Evidence for a further diffuse reversibly-bound layer forming at higher concentrations was also observed. Both the structure of the layer revealed by the neutron reflectometry data and the high water retention predicted by the QCM data suggest that there is a significant extent of protein unfolding upon adsorption. A lower extent of adsorption was seen on the chromium surfaces, although the adsorbed layer structures were similar, suggesting comparable adsorption mechanisms.

show abstract

Section: Introductionmentioning

confidence: 99%

Using Neutron Reflectometry to Discern the Structure of Fibrinogen Adsorption at the Stainless Steel/Aqueous Interface

et al. 2016

View full text Add to dashboard Cite

show abstract

“…SFG spectroscopy is well suited to study proteins at interfaces. [27][28][29] In the past SFG spectroscopy has frequently been used to investigate the hydration of PEGylated surfaces in presence or absence of proteins in the subphase. [30][31][32][33][34][35][36][37] Moreover, there are several in situ studies probing the water structure or protein backbone in the amide I region after adsorption on hydrophobic or hydrophilic surfaces.…”

Section: Introductionmentioning

confidence: 99%

Repelling and ordering: the influence of poly(ethylene glycol) on protein adsorption

Bernhard

Roeters

Franz

et al. 2017

Phys. Chem. Chem. Phys.

Self Cite

View full text Add to dashboard Cite

Development of new materials for drug delivery and biosensing requires the fine-tuning of interfacial properties. We report here the influence of the poly(ethylene glycol) (PEG) grafting density in model phospholipid monolayers on the adsorption behavior of bovine serum albumin and human fibrinogen, not only with respect to the amount of adsorbed protein, but also its orientational ordering on the surface. As expected, with increasing interfacial PEG density, the amount of adsorbed protein decreases up to the point where complete protein repellency is reached. However, at intermediate concentrations, the net orientation of adsorbed fibrinogen is highest. The different proteins respond differently to PEG, not only in the amount of protein adsorbed, but also in the manner that proteins adsorb. The results show that for specific cases, tuning the interfacial PEG concentration allows to guide the protein adsorption configuration, a feature sought after in materials for both biosensing and biomedical applications.

show abstract

“…15,17 Some of the methods that can provide information on adsorbed protein orientation and tertiary (and quaternary) structure include fluorescence, [18][19][20][21] time-of-flight secondary-ion mass spectrometry, [22][23][24] nuclear magnetic resonance spectroscopy (NMR), 25,26 and amino acid labeling/mass spectrometry (AAL/MS). [27][28][29][30][31] Methods for the determination of secondary structure of adsorbed proteins include Fourier transform infrared spectroscopy, 32,33 surface enhanced Raman scattering, 34,35 and circular dichroism spectropolarimetry (CD).…”

Section: Introductionmentioning

confidence: 99%

Experimental characterization of adsorbed protein orientation, conformation, and bioactivity

2015

View full text Add to dashboard Cite

Protein adsorption on material surfaces is a common phenomenon that is of critical importance in many biotechnological applications. The structure and function of adsorbed proteins are tightly interrelated and play a key role in the communication and interaction of the adsorbed proteins with the surrounding environment. Because the bioactive state of a protein on a surface is a function of the orientation, conformation, and accessibility of its bioactive site(s), the isolated determination of just one or two of these factors will typically not be sufficient to understand the structure-function relationships of the adsorbed layer. Rather a combination of methods is needed to address each of these factors in a synergistic manner to provide a complementary dataset to characterize and understand the bioactive state of adsorbed protein. Over the past several years, the authors have focused on the development of such a set of complementary methods to address this need. These methods include adsorbed-state circular dichroism spectropolarimetry to determine adsorptioninduced changes in protein secondary structure, amino-acid labeling/mass spectrometry to assess adsorbed protein orientation and tertiary structure by monitoring adsorption-induced changes in residue solvent accessibility, and bioactivity assays to assess adsorption-induced changes in protein bioactivity. In this paper, the authors describe the methods that they have developed and/or adapted for each of these assays. The authors then provide an example of their application to characterize how adsorption-induced changes in protein structure influence the enzymatic activity of hen eggwhite lysozyme on fused silica glass, high density polyethylene, and poly(methyl-methacrylate) as a set of model systems.

show abstract

SFG analysis of surface bound proteins: a route towards structure determination

Cited by 79 publications

References 100 publications

Using Neutron Reflectometry to Discern the Structure of Fibrinogen Adsorption at the Stainless Steel/Aqueous Interface

Using Neutron Reflectometry to Discern the Structure of Fibrinogen Adsorption at the Stainless Steel/Aqueous Interface

Repelling and ordering: the influence of poly(ethylene glycol) on protein adsorption

Experimental characterization of adsorbed protein orientation, conformation, and bioactivity

Contact Info

Product

Resources

About