Statistical inference in single molecule measurements of protein adsorption

Armstrong, Megan J.; Tsitkov, Stanislav; Hess, Henry

doi:10.1117/12.2290918

Cited by 3 publications

(3 citation statements)

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“…The probability that a protein has a surface lifetime of t or longer was determined by estimating the survival function, S ( t ). The measured residence times were used to construct an empirical cumulative distribution function and the complementary survival function using the Kaplan–Meier method as described in detail elsewhere . Briefly, the number of proteins with each given lifetime was normalized by the number of proteins with that lifetime or longer.…”

Section: Methodsmentioning

confidence: 99%

“…The measured residence times were used to construct an empirical cumulative distribution function and the complementary survival function using the Kaplan−Meier method as described in detail elsewhere. 46 Briefly, the number of proteins with each given lifetime was normalized by the number of proteins with that lifetime or longer. The normalization includes proteins who are still present in the last frame.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

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Power Law Behavior in Protein Desorption Kinetics Originating from Sequential Binding and Unbinding

et al. 2020

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The study of protein adsorption at the single molecule level has recently revealed that the adsorption is reversible, but with a long-tailed residence time distribution which can be approximated with a sum of exponential functions putatively related to distinct adsorption sites. Here it is proposed that the shape of the residence time distribution results from an adsorption process with sequential and reversible steps that contribute to overall binding strength resembling “zippering”. In this model, the survival function of the residence time distribution of single proteins varies from an exponential distribution for a single adsorption step to a power law distribution with exponent −1/2 for a large number of adsorption steps. The adsorption of fluorescently labeled fibrinogen to glass surfaces is experimentally studied with single molecule imaging. The experimental residence time distribution can be readily fit by the proposed model. This demonstrates that the observed long residence times can arise from stepwise adsorption rather than rare but strong binding sites and provides guidance for the control of protein adsorption to biomaterials.

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Section: Methodsmentioning

confidence: 99%

Section: ■ Experimental Sectionmentioning

confidence: 99%

Power Law Behavior in Protein Desorption Kinetics Originating from Sequential Binding and Unbinding

et al. 2020

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“…Molecular dynamics monitored using singlemolecule fluorescence imaging are conventionally observed from tens of milliseconds to minute time scales. This temporal range has monitored diffusion over micron distances and adsorption kinetics 58 but fails to resolve faster dynamics such as conformational changes, intermediate formation, and electron transfer reactions, along with longer dynamics such as fouling, degradation, formation of defects and unwanted products, and aging of stationary phases. 10 Therefore, expanding the temporal capabilities of single-molecule fluorescence microscopy to both shorter and longer scales should be pursued.…”

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confidence: 99%