Viscoelastic adlayers of collagen and lysozyme studied using quartz crystal microbalance with dissipation monitoring

Noji, Takashi; Taira, Masayuki; Saitoh, Setsuo; Sasaki, Kaori; Araki, Yoshimori

doi:10.1016/j.ijbiomac.2010.02.005

Cited by 9 publications

(6 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…For both methods of surface modification, the NAv layer appeared to be a dense, rigid continuum, as indicated by the minimal difference in Δ f values for consecutive higher sensor harmonics. This is in good agreement with results reported elsewhere for avidin-based systems and other similar proteins. − …”

Section: Resultssupporting

confidence: 92%

Surface Immobilization of Bio-Functionalized Cubosomes: Sensing of Proteins by Quartz Crystal Microbalance

et al. 2011

View full text Add to dashboard Cite

A strategy for tethering lipid liquid crystalline submicrometer particles (cubosomes) to a gold surface for the detection of proteins is reported. Time-resolved quartz crystal microbalance (QCM-D) was used to monitor the cubosome-protein interaction in real time. To achieve specific binding, cubosomes were prepared from the nonionic surfactant phytantriol, block-copolymer, Pluronic F-127, and a secondary biotinylated lipid, 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-[biotinyl(polyethyleneglycol)-2000], which enabled attachment of the particles to a neutravidin (NAv)-alkanethiol monolayer at the gold surface of the QCM sensor chip. A second set of cubosomes was further functionalized with addition of the glycolipid (G(M1)) to facilitate a specific binding uptake of the protein, cholera toxin B subunit (CT(B)), from solution. QCM-D confirmed the specificity of the cubosome-NAv binding. The analysis of titration experiments, also performed with QCM, suggests that an optimal concentration of cubosomes is required for the efficient packing of the particles at the surface: high cubosome concentrations lead to chaotic cubosome binding onto the surface, sterically inhibiting surface attachment, or require significant reorganization to permit uniform cubosome coverage. The methodology enabled the straightforward preparation of a complex nanostructured edifice, which was then used to specifically capture analyte proteins (cholera toxin B subunit or free NAv) from solution, supporting the potential for development of this approach as a biosensing platform.

show abstract

Section: Resultssupporting

confidence: 92%

Surface Immobilization of Bio-Functionalized Cubosomes: Sensing of Proteins by Quartz Crystal Microbalance

et al. 2011

View full text Add to dashboard Cite

show abstract

“…In the majority of studies, QCM-D is used to examine the adsorption of molecules from solution to a solid surface (an empty or coated sensor) from an aqueous solution that is flowed directly across the sensor. Lysozyme has been studied using QCM-D in various works using this approach including the investigation of the dependence of adsorption onto surfaces on ionic strength, pH value, or on the shape of the protein . Rheological properties have been analyzed using the QCM-D technique for enzyme immobilization or viscoelastic properties of adsorbed lysozyme films …”

Section: Introductionmentioning

confidence: 99%

Determination of Sorption Isotherm and Rheological Properties of Lysozyme Using a High-Resolution Humidity Scanning QCM-D Technique

Graf

Kocherbitov

2013

J. Phys. Chem. B

View full text Add to dashboard Cite

The high-resolution humidity scanning QCM-D technique enables investigation of hydration of soft matter films using a quartz crystal microbalance with dissipation monitoring (QCM-D) equipped with a humidity module. Based on a continuous increase of relative humidity, properties of soft matter films can be investigated depending on the water content of the surrounding atmosphere. Determination of complete water sorption isotherms is possible via analysis of the overtone dependence of the resonance frequencies. Rheological properties are monitored via measurement of the dissipation. The glass transition can be identified from the change of viscoelastic properties of the film reflected in changes of the dissipation. A high-resolution water sorption isotherm of lysozyme was measured and compared with results from water sorption calorimetry. Analysis of the rheological behavior during hydration of lysozyme films revealed the presence of two separate sharp transitions at the water activities 0.67 and 0.91, which are connected to the glass transition. In previous works, only the existence of a broad glass transition has been reported so far. Combining the QCM-D data with Raman scattering data presented earlier, a new mechanism of isothermal glass transition in lysozyme is proposed.

show abstract

“…The weight of chondroitin sulfate B was constant at 1b-3b. ，Xu らは pH と温度の影響について，Nezu らは pH と NaCl の影響について (Nezu et al, 2010…”

Section: 緒言unclassified

Effects of chondroitin sulfate B on the reconstitution of collagen fibrils

Yamamoto

Sasaki

2017

Transactions of the JSME (In Japanese)

View full text Add to dashboard Cite

Collagen fibrils were reconstituted in vitro from type I collagen solution. The reconstituted collagen fibrils and chondroitin sulfate B were deposited alternately. The adsorbed weight of the collagen fibrils and chondroitin sulfate B was measured using a quartz crystal microbalance (QCM) and their microstructure was observed using an atomic force microscope (AFM). The adsorbed weight of the collagen fibrils on the adsorption of collagen fibrils and chondroitin sulfate B alternately was significantly larger than that on the adsorption of collagen fibrils only. The adsorption of chondroitin sulfate B was observed on the surfaces of collagen fibrils. These results indicate that chondroitin sulfate B is effective on the reconstitution of collagen fibrils.

show abstract

Viscoelastic adlayers of collagen and lysozyme studied using quartz crystal microbalance with dissipation monitoring

Cited by 9 publications

References 26 publications

Surface Immobilization of Bio-Functionalized Cubosomes: Sensing of Proteins by Quartz Crystal Microbalance

Surface Immobilization of Bio-Functionalized Cubosomes: Sensing of Proteins by Quartz Crystal Microbalance

Determination of Sorption Isotherm and Rheological Properties of Lysozyme Using a High-Resolution Humidity Scanning QCM-D Technique

Effects of chondroitin sulfate B on the reconstitution of collagen fibrils

Contact Info

Product

Resources

About