Streamlined Synthesis and Assembly of a Hybrid Sensing Architecture with Solid Binding Proteins and Click Chemistry

Swift, Brian J. F.; Shadish, Jared A.; DeForest, Cole A.; Baneyx, François

doi:10.1021/jacs.7b00519

Cited by 15 publications

(17 citation statements)

References 40 publications

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“…32 Car9 is a SBP of amino acid sequence DSARGFKKPGKR that binds to the hydroxyl-, carbonyl-, and carboxylate-rich edges of graphitic nanostructures and exhibits a preference for sp 3 -hybridized carbon. 31 Following its original identification as a carbon-binding peptide, Car9 has been found to bind to silica, 33 enabling the creation of hybrid architectures, 34 and the affinity purification, 33,35 immobilization, 36 and microcontact printing 37 of proteins to which it is fused.…”

Section: ■ Introductionmentioning

confidence: 99%

Modeling the Cooperative Adsorption of Solid-Binding Proteins on Silica: Molecular Insights from Surface Plasmon Resonance Measurements

et al. 2019

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Combinatorially selected solid-binding peptides (SBPs) provide a versatile route for synthesizing advanced materials and devices, especially when they are installed within structurally or functionally useful protein scaffolds. However, their promise has not been fully realized because we lack a predictive understanding of SBP-material interactions. Thermodynamic and kinetic binding parameters obtained by fitting quartz crystal microbalance and surface plasmon resonance (SPR) data with the Langmuir model whose assumptions are rarely satisfied provide limited information on underpinning molecular interactions. Using SPR, we show here that a technologically useful SBP called Car9 confers proteins to which is fused a sigmoidal adsorption behavior modulated by partner identity, quaternary structure, and ionic strength. We develop a two-step cooperative model that accurately captures the kinetics of silica binding and provides insights into how SBP−SBP interactions, fused scaffold, and solution conditions modulate adsorption. Because cooperative binding can be converted to Langmuir adhesion by mutagenesis, our approach offers a path to identify and to better understand and design practically useful SBPs.

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Section: ■ Introductionmentioning

confidence: 99%

Modeling the Cooperative Adsorption of Solid-Binding Proteins on Silica: Molecular Insights from Surface Plasmon Resonance Measurements

et al. 2019

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“…The compositions and structures of proteins within cellular environments have evolved under biological selection criteria for diverse functionalities, including highly selective reactions, molecular or ion transport, and signaling, which often occur at high rates and support the viabilities of biological organisms. Recently, there has been significant progress in the engineering of proteins to have functionalities that are different from those of wild-type analogues by judiciously adjusting protein compositions through biomolecular mutagenesis processes (e.g., directed evolution). , Many such functionalities could be attractive for technological uses, such as chemical or biological sensing, catalysis, , separations, , bioanalytics, or energy conversion, though they are typically highly specific for certain substrates over a narrow range of conditions. The effective exploitation of proteins for nonbiological purposes often requires that proteins be extracted from native biological environments and stabilized in active forms within synthetic host materials.…”

Section: Introductionmentioning

confidence: 99%

Functionally Active Membrane Proteins Incorporated in Mesostructured Silica Films

et al. 2018

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A versatile synthetic protocol is reported that allows high concentrations of functionally active membrane proteins to be incorporated in mesostructured silica materials. Judicious selections of solvent, surfactant, silica precursor species, and synthesis conditions enable membrane proteins to be stabilized in solution and during subsequent co-assembly into silica-surfactant composites with nano- and mesoscale order. This was demonstrated by using a combination of non-ionic (n-dodecyl-β-D-maltoside or Pluronic P123), lipid-like (1,2-diheptanoyl-s,n-gycero-3-phosphocholine), and perfluoro-octanoate surfactants under mild acidic conditions to co-assemble the light-responsive transmembrane protein proteorhodopsin at concentrations up to 15 wt% into the hydrophobic regions of worm-like mesostructured silica materials in films. Small-angle X-ray scattering, electron paramagnetic resonance spectroscopy, and transient UV-visible spectroscopy analyses established that proteorhodopsin molecules in mesostructured silica films exhibited native-like function, as well as enhanced thermal stability compared to surfactant or lipid environments. The light absorbance properties and light-activated conformational changes of proteorhodopsin guests in mesostructured silica films are consistent with those associated with the native H+-pumping mechanism of these biomolecules. The synthetic protocol is expected to be general, as demonstrated also for the incorporation of functionally-active cytochrome c, a peripheral membrane protein enzyme involved in electron transport, into mesostructured silica-cationic surfactant films.

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“…Swift et al. [ 92 ] developed an aptasensor for the detection of chloramphenicol, which is an old antibiotic derived from Streptomyces venequelae [ 93 ]. The scaffold structure of the sfGFP provided an effective contact between a chloramphenicol-specific DNA aptamer, enabling optical detection of chloramphenicol in biological samples.…”

Section: Determination Of Pharmaceuticals and Drugsmentioning

confidence: 99%

Applications of scaffold-based advanced materials in biomedical sensing

Sarkhosh-Inanlou

Shafiei‐Irannejad

Azizi

et al. 2021

TrAC Trends in Analytical Chemistry

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There have been many efforts to synthesize advanced materials that are capable of real-time specific recognition of a molecular target, and allow the quantification of a variety of biomolecules. Scaffold materials have a porous structure, with a high surface area and their intrinsic nanocavities can accommodate cells and macromolecules. The three-dimensional structure (3D) of scaffolds serves not only as a fibrous structure for cell adhesion and growth in tissue engineering, but can also provide the controlled release of drugs and other molecules for biomedical applications. There has been a limited number of reports on the use of scaffold materials in biomedical sensing applications. This review highlights the potential of scaffold materials in the improvement of sensing platforms and summarizes the progress in the application of novel scaffold-based materials as sensor, and discusses their advantages and limitations. Furthermore, the influence of the scaffold materials on the monitoring of infectious diseases such as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and bacterial infections, was reviewed.

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Streamlined Synthesis and Assembly of a Hybrid Sensing Architecture with Solid Binding Proteins and Click Chemistry

Cited by 15 publications

References 40 publications

Modeling the Cooperative Adsorption of Solid-Binding Proteins on Silica: Molecular Insights from Surface Plasmon Resonance Measurements

Modeling the Cooperative Adsorption of Solid-Binding Proteins on Silica: Molecular Insights from Surface Plasmon Resonance Measurements

Functionally Active Membrane Proteins Incorporated in Mesostructured Silica Films

Applications of scaffold-based advanced materials in biomedical sensing

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