A Comprehensive Model of Multiprotein Adsorption on Surfaces

Lu, Chun Fang; Nadarajah, Arunan; Chittur, Krishnan K.

doi:10.1006/jcis.1994.1404

Cited by 66 publications

(55 citation statements)

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“…22,23 After being displaced, the desorbed probe reacts with the cDNA in solution to form a duplex as schematically shown in Figure 1C. Fluorescence enhancement was due to the unfavorable re-adsorption of the ds-DNA.…”

Section: Resultsmentioning

confidence: 99%

Mechanisms of DNA Sensing on Graphene Oxide

et al. 2013

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Adsorption of a fluorophore-labeled DNA probe by graphene oxide (GO) produces a sensor that gives fluorescence enhancement in the presence of its complementary DNA (cDNA). While many important analytical applications have been demonstrated, it remains unclear how DNA hybridization takes place in the presence of GO, hindering further rational improvement of sensor design. For the first time, we report a set of experimental evidence to reveal a new mechanism involving non-specific probe displacement followed by hybridization in the solution phase. In addition, we show quantitatively that only a small portion of the added cDNA molecules undergo hybridization while most are adsorbed by GO to play the displacement role. Therefore, it is possible to improve signaling by raising hybridization efficiency. A key innovation herein is using probes and cDNA with a significant difference in their adsorption energy by GO. This study offers important mechanistic insights into the GO/DNA system. At the same time, it provides simple experimental methods to study biomolecular reaction dynamics and mechanism on surface, which may be applied for many other biosensor systems.3

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Section: Resultsmentioning

confidence: 99%

Mechanisms of DNA Sensing on Graphene Oxide

et al. 2013

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“…Attraction among proteins is not included at this level of description, as it is small compared to proteinsurface interaction and the protein solution is stable 18 . The fibrinogen (Fib) in its folded conformation is rod-like.…”

Section: The Modelmentioning

confidence: 99%

“…Next, we identify R A = R H A , R I = R H I , and δ F = R H F , while R F is set by imposing that the experimental surface concentration found for Fib corresponds to its close packing configuration in the "standing up" conformation 18 . These conditions give R A = 3.55 nm, R I = 5.51 nm, R F = 9.29 nm and δ F = 11 nm.…”

Section: The Modelmentioning

confidence: 99%

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Understanding and modulating the competitive surface-adsorption of proteins through coarse-grained molecular dynamics simulations

2013

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It is now well accepted that cellular responses to materials in a biological medium reflect greatly the adsorbed biomolecular layer, rather than the material itself. Here, we study by molecular dynamic simulations the competitive protein adsorption on a surface (Vroman effect), i.e. the non-monotonic behavior of the amount of protein adsorbed on a surface in contact with plasma as a function of contact time and plasma concentration. We find a complex behavior, with regimes during which small and large proteins are not necessarily competing between them, but are both competing with others in solution. We show how the effect can be understood, controlled and inverted.

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“…Among various onchip analysis techniques, microchip electrophoresis (MCE), based on the separation principle of capillary electrophoresis (CE), has been widely used in the analysis of chemical and biogenic compounds because of its high separation efficiency, high-speed analysis and low consumption of samples in addition of the suitability for the parallel analysis on chips [5][6][7][8]. In the MCE analysis of biogenic compounds, especially proteins, however, it is well known that sample adsorption onto the surface of a separation microchannel due to electrostatic and/or hydrophobic interactions [9,10] often causes the reduction of the separation efficiency and the analytical reproducibility. Thus, various microchannel coating techniques have been developed to prevent the adsorption of biogenic compounds in MCE [11,12].…”

Section: Introductionmentioning

confidence: 99%

One-step immobilization of cationic polymer onto a poly(methyl methacrylate) microchip for high-performance electrophoretic analysis of proteins

Kitagawa

Kubota

Sueyoshi

et al. 2006

Science and Technology of Advanced Materials

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One-step covalent immobilization of poly(ethyleneimine) (PEI) onto poly(methyl methacrylate) (PMMA) substrates was investigated to achieve an efficient separation of basic proteins in microchip electrophoresis (MCE). The PEI-treated PMMA chip showed the anodic electroosmotic flow and its rate was almost kept stable during 32 days with over 50 runs. This longer stability of the prepared microchip indicated that the loss of PEI was successfully suppressed by the immobilization through the covalent bond. Furthermore, the PEI modification onto the PMMA chip could apparently reduce the surface adsorption of cationic proteins. In the MCE analysis on the PEImodified microchip, two proteins were successfully separated within 30 s only utilizing a separation length of 5 mm. While the migration time of the protein gradually increased during only four consecutive runs on an untreated PMMA chip, reproducible analyses were attained by using the PEI immobilized microchip. These results demonstrated that Coulombic repulsion force generated between cationic PEI and basic proteins could avoid the irreversible adsorption of the analytes onto the PMMA surface, which provided a highperformance analysis medium for biogenic compounds. r

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A Comprehensive Model of Multiprotein Adsorption on Surfaces

Cited by 66 publications

References 0 publications

Mechanisms of DNA Sensing on Graphene Oxide

Mechanisms of DNA Sensing on Graphene Oxide

Understanding and modulating the competitive surface-adsorption of proteins through coarse-grained molecular dynamics simulations

One-step immobilization of cationic polymer onto a poly(methyl methacrylate) microchip for high-performance electrophoretic analysis of proteins

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