Sum Frequency Generation Studies on Bioadhesion: Elucidating the Molecular Structure of Proteins at Interfaces

Clair, Stéphanie V. Le; Nguyen, Khoi Tan; Chen, Zhan

doi:10.1080/00218460902996374

Cited by 20 publications

(9 citation statements)

References 169 publications

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“…By contrast, mfp-3 is an adhesive primer for mussel adhesion and it should have underwater adhesion ability regardless of surface chemistry. Recent studies aided by SFG vibrational spectroscopy and CD strongly support the notion that mfp-3 adopts different conformations at various interfaces depending on specific chemical interactions [41][42][43]. Therefore, relatively stronger adhesion ability of mfp-3 to the tested substrates than mfp-1 and mfp-5 is partially due to a superior conformational adaptability of mfp-3 on the different surface chemistries.…”

Section: Psmentioning

confidence: 85%

Adhesion of mussel foot proteins to different substrate surfaces

Danner

Waite

et al. 2013

J. R. Soc. Interface.

281

243

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Mussel foot proteins (mfps) have been investigated as a source of inspiration for the design of underwater coatings and adhesives. Recent analysis of various mfps by a surface forces apparatus (SFA) revealed that mfp-1 functions as a coating, whereas mfp-3 and mfp-5 resemble adhesive primers on mica surfaces. To further refine and elaborate the surface properties of mfps, the force-distance profiles of the interactions between thin mfp (i.e. mfp-1, mfp-3 or mfp-5) films and four different surface chemistries, namely mica, silicon dioxide, polymethylmethacrylate and polystyrene, were measured by an SFA. The results indicate that the adhesion was exquisitely dependent on the mfp tested, the substrate surface chemistry and the contact time. Such studies are essential for understanding the adhesive versatility of mfps and related/similar adhesion proteins, and for translating this versatility into a new generation of coatings and (including in vivo) adhesive materials.

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Section: Psmentioning

confidence: 85%

Adhesion of mussel foot proteins to different substrate surfaces

Danner

Waite

et al. 2013

J. R. Soc. Interface.

281

243

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“…74, 7572, 76 Polarization dependent SFG measurements, where the polarizations of the incident infrared and visible beams and the detected SFG photons are varied between s- and p-polarization, allow one to probe protein orientation in membranes and on surfaces 69, 74, 75, 77, 78 .…”

Section: Sum Frequency Generation Spectroscopy For Protein Studiesmentioning

confidence: 99%

“…72,[74][75][76] Polarization dependent SFG measurements, where the polarizations of the incident infrared and visible beams and the detected SFG photons are varied between s-and p-polarization, allow one to probe protein orientation in membranes and on surfaces. 69,74,75,77,78 Fig. 2 shows, an example for a quantitative study of the orientation of LKa14 peptides adsorbed onto polystyrene surfaces.…”

Section: Sum Frequency Generation Spectroscopy For Protein Studiesmentioning

confidence: 99%

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

Weidner

Castner

2013

Phys. Chem. Chem. Phys.

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The surface of a material is rapidly covered with proteins once that material is placed in a biological environment. The structure and function of these bound proteins play a key role in the interactions and communications of the material with the biological environment. Thus, it is crucial to gain a molecular level understanding of surface bound protein structure. While X-ray diffraction and solution phase NMR methods are well established for determining the structure of proteins in the crystalline or solution phase, there is not a corresponding single technique that can provide the same level of structural detail about proteins at surfaces or interfaces. However, recent advances in sum frequency generation (SFG) vibrational spectroscopy have significantly increased our ability to obtain structural information about surface bound proteins and peptides. A multi-technique approach of combining SFG with (1) protein engineering methods to selectively introduce mutations and isotopic labels, (2) other experimental methods such as time-of-flight secondary ion mass spectrometry (ToF-SIMS) and near edge x-ray absorption fine structure (NEXAFS) to provide complementary information, and (3) molecular dynamic (MD) simulations to extend the molecular level experimental results is a particularly promising route for structural characterization of surface bound proteins and peptides. By using model peptides and small proteins with well-defined structures, methods have been developed to determine the orientation of both backbone and side chains to the surface.

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“…Recently, surface-sensitive sum frequency generation vibrational spectroscopy (SFG) has been applied to the study of proteins and peptides at interfaces in situ. − Early results demonstrated the superb interfacial sensitivity of SFG; however, the interpretation of vibrational spectra in terms of molecular structure or orientation generally requires assumptions about the native crystal structure of the protein. These methods are not able to provide atomically detailed structures or to assess orientation in the event of significant changes in structure.…”

Section: Introductionmentioning

confidence: 99%

Surface Orientation of Magainin 2: Molecular Dynamics Simulation and Sum Frequency Generation Vibrational Spectroscopic Studies

2010

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We combined molecular dynamics based free energy calculations with Sum Frequency Generation (SFG) spectroscopy to study the orientational distribution of solvated peptides near hydrophobic surfaces. Using a simplified atomistic model of the polystyrene (PS) surface, molecular dynamics simulations have been applied to compute the orientational probability of an α-helical peptide, magainin 2, with respect to the PS/water interface. Free energy calculations revealed that the preferred (horizontal) peptide orientation was driven by the favorable interactions between the hydrophobic PS surface and hydrophobic residues on the helix, and additional simulations examined the importance of small aggregate formation. Concentration-dependent measurements obtained via SFG vibrational spectroscopy suggest that at very low peptide concentrations, magainin molecules tend to lie down at the PS/solution interface, which correlates well with the simulation results. When the concentration is increased, peptides exhibit behavior not captured by MD simulations using single helical peptides. A combination of simulations and experiments was shown to yield more reliable results with molecular-level insights into interaction between peptides and polymer surfaces.

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Sum Frequency Generation Studies on Bioadhesion: Elucidating the Molecular Structure of Proteins at Interfaces

Cited by 20 publications

References 169 publications

Adhesion of mussel foot proteins to different substrate surfaces

Adhesion of mussel foot proteins to different substrate surfaces

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

Surface Orientation of Magainin 2: Molecular Dynamics Simulation and Sum Frequency Generation Vibrational Spectroscopic Studies

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