Biomolecular Structure at Solid–Liquid Interfaces As Revealed by Nonlinear Optical Spectroscopy

Roy, Sandra; Covert, Paul A.; Fitzgerald, William; Hore, Dennis K.

doi:10.1021/cr400418b

Cited by 106 publications

(101 citation statements)

References 254 publications

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“…[18][19][20] It has been extensively applied to study the molecular structures of polymers 21 and biomolecules 22,23 at various interfaces and has proven particularly powerful in revealing polymer/water interfacial structures 24, 25 in ambient environments. Furthermore, the detailed structural information of interfacial water can be extracted from SFG data.…”

Section: Introductionmentioning

confidence: 99%

Probing the Surface Hydration of Nonfouling Zwitterionic and PEG Materials in Contact with Proteins

Leng

Hung

Sun

et al. 2015

ACS Appl. Mater. Interfaces

241

244

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Zwitterionic polymers and poly(ethylene glycol) (PEG) have been reported as promising nonfouling materials, and strong surface hydration has been proposed as a significant contributor to the nonfouling mechanism. Better understanding of the similarity and difference between these two types of materials in terms of hydration and protein interaction will benefit the design of new and effective nonfouling materials. In this study, sum frequency generation (SFG) vibrational spectroscopy was applied for in situ and real-time assessment of the surface hydration of the sulfobetaine methacrylate (SBMA) and oligo(ethylene glycol) methacrylate (OEGMA) polymer brushes, denoted as pSBMA and pOEGMA, in contact with proteins. Whereas a majority of strongly hydrogen-bonded water was observed at both pSBMA and pOEGMA surfaces, upon contact with proteins, the surface hydration of pSBMA remained unaffected, but the water ordering at the pOEGMA surface was disturbed. The effects of free sulfobetaine, free PEG chains with two different molecular weights, and PEG coated gold nanoparticles on the surface hydration of proteins were investigated. The results indicated that free sulfobetaine could strengthen the protein hydration layer, but free PEG chains greatly disrupt the protein hydration layer and likely directly interact with the protein molecules. In contrast to free PEG, the PEG chains anchored on the nanoparticles behave similarly to the pOEGMA surface and could induce strong hydrogen bonding of the water molecules at the protein surfaces.

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Section: Introductionmentioning

confidence: 99%

Probing the Surface Hydration of Nonfouling Zwitterionic and PEG Materials in Contact with Proteins

Leng

Hung

Sun

et al. 2015

ACS Appl. Mater. Interfaces

241

244

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.

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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.

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“…[17][18][19][20][21] Clearly, D1 is a function of the (  ) pair, so a single D1 cannot warrant a unique solution to both   and.…”

Section: Introductionmentioning

confidence: 99%

Solving the “Magic Angle” Challenge in Determining Molecular Orientation Heterogeneity at Interfaces

Xiong

2016

J. Phys. Chem. C

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It is critical to determine conformations of molecular monolayers in order to understand and control their functions and properties, such as efficiencies of self-assembly-based biosensors and turnover frequency of surface-bound electrocatalysts. However, surface molecules of the monolayers can adopt conformations with many different orientations. Thus, it is necessary to describe the orientations of surface molecular monolayers using both mean tilt angle and orientational distribution, which together we refer as orientation heterogeneity. Orientation heterogeneity is difficult to measure. In most cases, in order to calculate the mean tilt angle, it is assumed that the orientational distribution is narrow. This assumption causes ambiguities in determining the mean tilt angle, and loss of orientational distribution information, which is known as the "magic angle" challenge. Using heterodyne two-dimensional vibrational sum frequency generation (HD 2D VSFG) spectroscopy, we report a novel method to solve the "magic angle" challenge, by simultaneously measuring mean tilt angle and orientational distribution of molecular monolayers. We applied this new method to a CO2 reduction catalyst/gold interface and found that the catalysts formed a monolayer with a mean tilt angle between its quasi-C3 symmetric axis and the surface normal of 53°, with 5° orientational distribution. The narrow orientational distribution indicates that the surface molecules are rigid, which sample only limited configurations for facilitating a reaction, because of the short anchoring groups. Although applied to a specific system, this method is a general way to determine the orientation heterogeneity of an ensemble-averaged molecular interface.3

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Biomolecular Structure at Solid–Liquid Interfaces As Revealed by Nonlinear Optical Spectroscopy

Cited by 106 publications

References 254 publications

Probing the Surface Hydration of Nonfouling Zwitterionic and PEG Materials in Contact with Proteins

Probing the Surface Hydration of Nonfouling Zwitterionic and PEG Materials in Contact with Proteins

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

Solving the “Magic Angle” Challenge in Determining Molecular Orientation Heterogeneity at Interfaces

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