Detection of streptavidin–biotin intermediate metastable states at the single-molecule level using high temporal-resolution atomic force microscopy

Mondarte, Evan Angelo Quimada; Maekawa, Tatsuhiro; Nyu, Takashi; Tahara, Hiroyuki; Lkhamsuren, Ganchimeg; Hayashi, T.

doi:10.1039/c9ra04106k

Cited by 8 publications

(7 citation statements)

References 40 publications

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“…We performed fast force mapping experiments at a pixel rate of 200 Hz. 33 Fig. 5a shows typical force curves collected from one pixel during the wave-like motion of the cantilever.…”

Section: Resultsmentioning

confidence: 99%

Dendronized oligoethylene glycols with phosphonate tweezers for cell-repellent coating of oxide surfaces: coarse-scale and nanoscopic interfacial forces

et al. 2021

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“…We performed fast force mapping experiments at a pixel rate of 200 Hz. 33 Fig. 5a shows typical force curves collected from one pixel during the wave-like motion of the cantilever.…”

Section: Resultsmentioning

confidence: 99%

Dendronized oligoethylene glycols with phosphonate tweezers for cell-repellent coating of oxide surfaces: coarse-scale and nanoscopic interfacial forces

et al. 2021

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“…This is attributed to the hydration of the zwitterionic terminal groups that provided the energetic cost for the aggregation of biomolecules. Our study could provide information for other systems such as biosensors toward understanding the influence of various types of nano-crowding at the interface to binding activities and kinetics of complementary proteins. ,, …”

Section: Discussionmentioning

confidence: 99%

“…Our study could provide information for other systems such as biosensors toward understanding the influence of various types of nano-crowding at the interface to binding activities and kinetics of complementary proteins. 5,6,64 Furthermore, proteins are also essentially bio-inert, similar to an SB surface, due to a surrounding hydration layer. 29,65,66 Therefore, this water covering plays a role in the specific recognition between complementary proteins (e.g., receptor and ligand) under crowded conditions by inhibiting nonspecific interactions.…”

Section: ■ Summary and Conclusionmentioning

confidence: 99%

“…Targeted interactions for protein transport and cellular communications are ubiquitous in a living body. One case in point is the transmembrane protein-mediated recognition of vesicles to specific physiological surfaces. − This specific binding is at the base of several biological processes and happens with a considerably low incidence of non-specific binding with other non-target molecules. ,− This phenomenon propelled the ongoing advancement of introducing artificial particles into living bodies to aid in investigating issues in the field of biomedicine. These particles span in various types from inorganic to polymeric, to biomimetic (particularly, liposomal), which are used for bio-imaging and drug delivery. − The surfaces of these materials are enforced with functional moieties or recognition units to facilitate the targeted approach and specifically bind to the intended biomolecular locations.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2022

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We investigated a viscous protein layer formed on self-assembled monolayers (SAMs) in crowded biological environments. The results were obtained through force spectroscopic measurements using colloidal probes and substantiated by exhaustive analysis using a quartz crystal microbalance with an energy dissipation technique. A hydrophobic SAM of n-octanethiol (C8 SAM) in bovine serum albumin (BSA) solution is buried under an adlayer of denatured BSA molecules and an additional viscous interphase layer that is five times more viscous than the bulk solution. C8 SAMs in fetal bovine serum induced a formation of a thicker adsorbed protein layer but with no observable viscous interphase layer. These findings show that a fouling surface is essentially inaccessible to any approaching molecules and thus has a new biological and physical identity arising from its surrounding protein layers. In contrast, the SAMs composed of sulfobetaine-terminated alkanethiol proved to be sufficiently protein-resistant and bio-inert even under crowded conditions due to a protective barrier of its interfacial water, which has implications in the accurate targeting of artificial particles for drug delivery and similar applications by screening any non-specific interactions. Finally, our strategies provide a platform for the straightforward yet effectual in vitro characterization of diverse types of surfaces in the context of targeted interactions in crowded biological environments.

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“…We assume that the reaction pathway along the reaction coordinate may depend on the loading speed because of the structural flexibility of SA. (45) To explain this discrepancy clearly, an analysis to acquire a detailed picture of the unbinding process using molecular simulations is underway.…”

Section: Single-molecule Force Spectroscopymentioning

confidence: 99%

Lab on a Tip: Atomic Force Microscopy as a Versatile Analytical Tool for Nano-bioscience

Mondarte¹,

Tahara²,

Suthiwanich³

et al. 2021

Sensors and Materials

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Scanning probe microscopy (SPM) is a powerful method for visualizing the structure of materials at the nanoscale. In particular, atomic force microscopy (AFM) has become one of the most used analytical tools in various fields such as physics, chemistry, and biology. Here, we introduce representative works in nano-bioscience. First, we look back on the history of SPM and introduce the application of AFM in this field. Next, we review surface force and singlemolecule force measurements, which unveiled molecular processes at biointerfaces. Surface force measurements revealed the mechanism underlying the macroscopically observed protein and cell resistance of artificial monolayers and biomolecules. Meanwhile, single-molecule force spectroscopy has enabled researchers to explore the complex interaction of biomolecules from a microscopic viewpoint. These findings will contribute not only to the fundamental understanding of biomolecular processes but also to the design of new nano-biodevices.

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Detection of streptavidin–biotin intermediate metastable states at the single-molecule level using high temporal-resolution atomic force microscopy

Abstract: Energy landscape illustration from the streptavidin–biotin binding dynamics observed in high temporal-resolution AFM.

Cited by 8 publications

References 40 publications

Dendronized oligoethylene glycols with phosphonate tweezers for cell-repellent coating of oxide surfaces: coarse-scale and nanoscopic interfacial forces

Dendronized oligoethylene glycols with phosphonate tweezers for cell-repellent coating of oxide surfaces: coarse-scale and nanoscopic interfacial forces

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

Lab on a Tip: Atomic Force Microscopy as a Versatile Analytical Tool for Nano-bioscience

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