Interphase Protein Layers Formed on Self-Assembled Monolayers in Crowded Biological Environments: Analysis by Surface Force and Quartz Crystal Microbalance Measurements

Mondarte, Evan Angelo Quimada; Zamarripa, Elisa Margarita Mendoza; Chang, Ryongsok; Wang, Fan; Song, S. N.; Tahara, Hiroyuki; Hayashi, T.

doi:10.1021/acs.langmuir.1c02312

Cited by 9 publications

(7 citation statements)

References 65 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We previously reported that a layer of denatured protein molecules with a thickness of about 10 nm is formed on protein-adsorbing surfaces. 55 We concluded that this layer resulted in the local change in the refractive index at the interface.…”

Section: ■ Results and Discussionmentioning

confidence: 85%

“…Therefore, the difference in the response in serum (between 0 and 540 s) is due to the difference in the accumulation and conformational change of the protein molecules. We previously reported that a layer of denatured protein molecules with a thickness of about 10 nm is formed on protein-adsorbing surfaces . We concluded that this layer resulted in the local change in the refractive index at the interface.…”

Section: Resultsmentioning

confidence: 87%

See 1 more Smart Citation

Prediction of Serum Adsorption onto Polymer Brush Films by Machine Learning

Palai

Tahara

Chikami

et al. 2022

ACS Biomater. Sci. Eng.

Self Cite

View full text Add to dashboard Cite

Using machine learning based on a random forest (RF) regression algorithm, we attempted to predict the amount of adsorbed serum protein on polymer brush films from the films’ physicochemical information and the monomers’ chemical structures constituting the films using a RF model. After the training of the RF model using the data of polymer brush films synthesized from five different types of monomers, the model became capable of predicting the amount of adsorbed protein from the chemical structure, physicochemical properties of monomer molecules, and structural parameters (density and thickness of the films). The analysis of the trained RF quantitatively provided the importance of each structural parameter and physicochemical properties of monomers toward serum protein adsorption (SPA). The ranking for the significance of the parameters agrees with our general understanding and perception. Based on the results, we discuss the correlation between brush film’s physical properties (such as thickness and density) and SPA and attempt to provide a guideline for the design of antibiofouling polymer brush films.

show abstract

Section: ■ Results and Discussionmentioning

confidence: 85%

Section: Resultsmentioning

confidence: 87%

Prediction of Serum Adsorption onto Polymer Brush Films by Machine Learning

Palai

Tahara

Chikami

et al. 2022

ACS Biomater. Sci. Eng.

Self Cite

View full text Add to dashboard Cite

show abstract

“…A viscous protein layer formed over self-assembled monolayers (SAMs) was investigated by Mondarte et al [ 42 ] in a BSA-crowded biological environment. The researchers used two SAM layers—one composed of 1-octane thiol (C8 SAM) and the second composed of zwitterionic sulfobetaine (SB)-terminated alkanethiol (SB SAM).…”

Section: Biological Sensorsmentioning

confidence: 99%

A Review of Quartz Crystal Microbalance for Chemical and Biological Sensing Applications

2023

View full text Add to dashboard Cite

Humans are fundamentally interested in monitoring and understanding interactions that occur in and around our bodies. Biological interactions within the body determine our physical condition and can be used to improve medical treatments and develop new drugs. Daily life involves contact with numerous chemicals, ranging from household elements, naturally occurring scents from common plants and animals, and industrial agents. Many chemicals cause adverse health and environmental effects and require regulation to prevent pollution. Chemical detection is critically important for food and environmental quality control efforts, medical diagnostics, and detection of explosives. Thus, sensitive devices are needed for detecting and discriminating chemical and biological samples. Compared to other sensing devices, the Quartz Crystal Microbalance (QCM) is well-established and has been considered and sufficiently sensitive for detecting molecules, chemicals, polymers, and biological assemblies. Due to its simplicity and low cost, the QCM sensor has potential applications in analytical chemistry, surface chemistry, biochemistry, environmental science, and other disciplines. QCM detection measures resonate frequency changes generated by the quartz crystal sensor when covered with a thin film or liquid. The quartz crystal is sandwiched between two metal (typically gold) electrodes. Functionalizing the electrode’s surface further enhances frequency change detection through to interactions between the sensor and the targeted material. These sensors are sensitive to high frequencies and can recognize ultrasmall masses. This review will cover advancements in QCM sensor technologies, highlighting in-sensor and real-time analysis. QCM-based sensor function is dictated by the coating material. We present various high-sensitivity coating techniques that use this novel sensor design. Then, we briefly review available measurement parameters and technological interventions that will inform future QCM research. Lastly, we examine QCM’s theory and application to enhance our understanding of relevant electrical components and concepts.

show abstract

“…It is well known that protein adsorption from HS onto solid surfaces has complex kinetics with faster adsorbing components with low affinity gradually being replaced by more slowly adsorbing species with high affinity (Vroman effect , ). Also, for the incubation times with the coating proteins used in Figure , coating formation had stabilized almost, but not completely yet.…”

Section: Resultsmentioning

confidence: 99%

Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces

et al. 2023

View full text Add to dashboard Cite

We analyze modularity for a B-M-E triblock protein designed to selfassemble into antifouling coatings. Previously, we have shown that the design performs well on silica surfaces when B is taken to be a silica-binding peptide, M is a thermostable trimer domain, and E is the uncharged elastin-like polypeptide (ELP), E = (GSGVP) 40 .Here, we demonstrate that we can modulate the nature of the substrate on which the coatings form by choosing different solid-binding peptides as binding domain B and that we can modulate antifouling properties by choosing a different hydrophilic block E. Specifically, to arrive at antifouling coatings for gold surfaces, as binding block B we use the gold-binding peptide GBP1 (with the sequence MHGKTQATSGTIQS), while we replace the antifouling blocks E by zwitterionic ELPs of different lengths, E Z n = (GDGVP-GKGVP) n/2 , with n = 20, 40, or 80. We find that even the B-M-E proteins with the shortest E blocks make coatings on gold surfaces with excellent antifouling against 1% human serum (HS) and reasonable antifouling against 10% HS. This suggests that the B-M-E triblock protein can be easily adapted to form antifouling coatings on any substrate for which solid-binding peptide sequences are available.

show abstract

Interphase Protein Layers Formed on Self-Assembled Monolayers in Crowded Biological Environments: Analysis by Surface Force and Quartz Crystal Microbalance Measurements

Cited by 9 publications

References 65 publications

Prediction of Serum Adsorption onto Polymer Brush Films by Machine Learning

Prediction of Serum Adsorption onto Polymer Brush Films by Machine Learning

A Review of Quartz Crystal Microbalance for Chemical and Biological Sensing Applications

Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces

Contact Info

Product

Resources

About