Study of Glucose Binding Protein Encapsulated Gold Nanoclusters by Molecular Dynamic Simulation

2019 ◽  
Vol 948 ◽  
pp. 133-139
Author(s):  
Boy Marsaputra Panjaitan ◽  
Karina Kubiak-Ossowska ◽  
David Birch ◽  
Yu Chen
Keyword(s):  
Md Simulation ◽  
Glucose Sensor ◽  
Binding Protein ◽  
Gold Nanoclusters ◽  
High Sensitivity ◽  
Nucleation Site ◽  
Fluorescent Properties ◽  
Glucose Binding ◽  
Sensitivity And Selectivity ◽  
Glucose Binding Protein

Protein encapsulated gold nanoclusters has attracted great attention for their excellent fluorescent properties and potential biomedical applications. Glucose Binding Protein (GBP) has a high sensitivity and selectivity to glucose binding that makes them ideal for biosensor development. It is anticipated that GBP encapsulated gold nanoclusters could be a promising glucose sensor. Here we investigated the growth of gold nanoclusters in GBP using Molecular Dynamics (MD) simulation. To facilitation the nucleation of gold nanoclusters at specific sites, cysteine mutations were introduced in GBP. It is found that the nucleation site of gold nanoclusters inside mutant GBP are different from those in native GBP. Gold nanoclusters were formed near the mutated cysteine and tyrosine residues. Glucose remained in the binding site of a mutant GBP with gold nanoclusters although no conformational change was observed in MD simulation, similar to a native GBP. This work suggests the possibility of growing gold nanoclusters in the designed site within GBP and a new glucose sensor based on mutated GBP protected gold nanoclusters.

scholarly journals Structural Analysis of a Genetically Encoded FRET Biosensor by SAXS and MD Simulations

Sensors ◽  
2021 ◽  
Vol 21 (12) ◽  
pp. 4144
Author(s):  
Ines Reinartz ◽  
Mona Sarter ◽  
Julia Otten ◽  
Henning Höfig ◽  
Martina Pohl ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Ligand Binding ◽  
Conformational Changes ◽  
Glucose Sensor ◽  
Binding Protein ◽  
Coarse Grained ◽  
Radius Of Gyration ◽  
Glucose Binding ◽  
Donor And Acceptor ◽  
Glucose Binding Protein

Inspired by the modular architecture of natural signaling proteins, ligand binding proteins are equipped with two fluorescent proteins (FPs) in order to obtain Förster resonance energy transfer (FRET)-based biosensors. Here, we investigated a glucose sensor where the donor and acceptor FPs were attached to a glucose binding protein using a variety of different linker sequences. For three resulting sensor constructs the corresponding glucose induced conformational changes were measured by small angle X-ray scattering (SAXS) and compared to recently published single molecule FRET results (Höfig et al., ACS Sensors, 2018). For one construct which exhibits a high change in energy transfer and a large change of the radius of gyration upon ligand binding, we performed coarse-grained molecular dynamics simulations for the ligand-free and the ligand-bound state. Our analysis indicates that a carefully designed attachment of the donor FP is crucial for the proper transfer of the glucose induced conformational change of the glucose binding protein into a well pronounced FRET signal change as measured in this sensor construct. Since the other FP (acceptor) does not experience such a glucose induced alteration, it becomes apparent that only one of the FPs needs to have a well-adjusted attachment to the glucose binding protein.

One-Dimensional Fluorescent Nanosized-Diamond Nanowires with Fluorescent Detection of Vitamin B12

NANO ◽  
2019 ◽  
Vol 14 (07) ◽  
pp. 1950084 ◽  
Author(s):  
Jilong Wang ◽  
Siheng Su ◽  
Jingjing Qiu ◽  
Shiren Wang
Keyword(s):  
Electron Microscopy ◽  
Photoelectron Spectroscopy ◽  
High Sensitivity ◽  
Anodic Aluminum Oxide Template ◽  
Fluorescent Detection ◽  
Dimensional Structure ◽  
Fluorescent Properties ◽  
One Dimensional ◽  
Sensitivity And Selectivity ◽  
The One

In this paper, a novel and facile method to achieve fluorescent nanosized-diamond based nanowire (NW) is reported. One-dimensional (1D) organic NW has received tremendous attention due to its superior chemical functionality and size-, shape-, and material-dependent properties. In addition, nanosized-diamond is comprehensively studied and investigated due to superior tunable fluorescent properties, cost-effectiveness, facile manufacturing and high biocompatibility. Through thermal treatment, sulfur-modified nanosized-diamond was fabricated by mixing oxidized nanosized-diamond and dibenzyl disulfide at 900∘C. Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS) and zeta potential were employed to characterize sulfur-modified nanosized-diamond. After that, porous anodic aluminum oxide template-assisted cathodic electrophoretic deposition method was used to achieve sulfur-modified nanosized-diamond NW. Scanning electron microscopy and transmission electron microscopy were applied to present the one-dimensional structure of the NWs. The optical properties of sulfur nanosized-diamond NW were characterized via ultraviolet-visible spectroscopy and photoluminescence spectroscopy. Finally, the as-synthesized sulfur-modified nanosized-diamond NW-based optical sensor was fabricated to detect vitamin B[Formula: see text] with high sensitivity and selectivity.

Labeling of a glucose binding protein in the rabbit intestinal brush border membrane

1978 ◽  
Vol 56 (5) ◽  
pp. 760-770 ◽  
Author(s):  
J. Lemaire ◽  
D. Maestracci
Keyword(s):  
Molecular Weight ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Binding Protein ◽  
Electrophoretic Pattern ◽  
Protein Band ◽  
Relative Mobility ◽  
Intestinal Brush Border ◽  
Glucose Binding ◽  
Glucose Binding Protein

Using a double labeling method based on the method of Thomas (Thomas, L. 1973. Isolation of N-ethylmaleimide-labeled phloridzin-sensitive D-glucose binding protein of brash border membrane from rat kidney cortex. Biochim. Biophys. Acta, 291, 454–464.), with radioactive N-ethylmaleimide ([3H]NEM and [14C]NEM) in the presence and absence of D-glucose, a protein band which is periodic acid – Schiff staining insensitive and which has a relative mobility (Rm) of 0.55 (corresponding to a molecular weight of 51 000 daltons) as determined by sodium dodecyl sulfate (SDS) electrophoresis was labeled preferentially.When radioactive p-hydroxymercuriphenylsulfonate ([203Hg]PCMBS) is used in the presence and absence of D-glucose, as described by Smith et al. (SMITH, M. W., FERGUSON, D. R., and BURTON, K. A. 1975. Glucose- and phloridzin-protected thiol groups in pig intestinal brush border membranes. Biochern. J. 147, 617–619.), a protein band which has a relative mobility of 0.62 and a corresponding molecular weight of 42 000 daltons was labeled.Control experiments have shown that increasing concentrations of nonradioactive NEM (0.1–5.0 mM) do not substantially modify the electrophoretic pattern of SDS-solubilized brush border membrane. Nonradioactive PCMBS (0.1–10 mM), on the other hand, modifies the electrophoretic pattern and especially causes a change in relative mobility of the 0.55 protein band which migrates after 1 mM PCMBS treatment with a Rm of 0.62.The effect of 1 mM PCMBS can be reversed by adding L-cysteine or dithiotreitol.Actin extracted from rabbit muscle migrates with the same Rm as the 0.55 protein band in our electrophoretic conditions.

Pressure effect on the stability and the conformational dynamics of the D-Galactose/D-Glucose-binding protein from Escherichia coli

2005 ◽  
Vol 62 (1) ◽  
pp. 193-201 ◽  
Author(s):  
Anna Marabotti ◽  
Petr Herman ◽  
Maria Staiano ◽  
Antonio Varriale ◽  
Marcella de Champdoré ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pressure Effect ◽  
Binding Protein ◽  
Conformational Dynamics ◽  
Glucose Binding ◽  
The Stability ◽  
Glucose Binding Protein

scholarly journals A highly selective and sensitive fluorescent probe for lactate dehydrogenase based on ultrabright adenosine monophosphate capped gold nanoclusters

RSC Advances ◽  
2017 ◽  
Vol 7 (22) ◽  
pp. 13438-13443 ◽  
Author(s):  
Jiao Liu ◽  
Hong-Wei Li ◽  
Yuqing Wu
Keyword(s):  
Lactate Dehydrogenase ◽  
Detection Limit ◽  
Fluorescent Probe ◽  
Fluorescence Probe ◽  
Gold Nanoclusters ◽  
High Sensitivity ◽  
Adenosine Monophosphate ◽  
Low Detection Limit ◽  
Sensitivity And Selectivity

The ultrabright AuNCs@AMP are used as fluorescence probe to detect lactate dehydrogenase (LDH) with high sensitivity and selectivity, showing an extremely low detection limit of 0.2 nM (26 pg μL−1, 0.8 U L−1).

Preformulation Characterization, Stabilization, and Formulation Design for the Acrylodan-Labeled Glucose-Binding Protein SM4-AC

2017 ◽  
Vol 106 (5) ◽  
pp. 1197-1210 ◽  
Author(s):  
Neha Sahni ◽  
Rajoshi Chaudhuri ◽  
John M. Hickey ◽  
Prakash Manikwar ◽  
Ajit D’Souza ◽  
...  
Keyword(s):  
Binding Protein ◽  
Formulation Design ◽  
Glucose Binding ◽  
Glucose Binding Protein

Substrate specificity of the high-affinity glucose transport system of Pseudomonas aeruginosa

1993 ◽  
Vol 39 (7) ◽  
pp. 722-725 ◽  
Author(s):  
John L. Wylie ◽  
Elizabeth A. Worobec
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Glucose Transport ◽  
Transport System ◽  
Binding Protein ◽  
High Affinity ◽  
Glucose Binding ◽  
Glucose Transport System ◽  
Glucose Binding Protein

Specificity of the high-affinity glucose transport system of Pseudomonas aeruginosa was examined. At a concentration of [14C]glucose near the Vmax of the system, inhibition by maltose, galactose, and xylose was detected. This inhibition is similar to that detected in earlier in vivo studies and correlates with the known specificity of OprB, a glucose-specific porin of P. aeruginosa. At a level of [14C]glucose 100 times lower, only unlabelled glucose inhibited uptake to any extent. This matches the known in vitro specificity of the periplasmic glucose binding protein. These findings were used to explain the discrepancy between earlier in vivo and in vitro results reported in the literature.Key words: Pseudomonas aeruginosa, glucose transport, OprB, glucose binding protein.

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