High-resolution identification of human adiponectin oligomers and regulation by pioglitazone in type 2 diabetic patients

Mashalidis, Ellene H.; Briggs, David B.; Zhou, Mowei; Vergara, Ashley M.; Chhun, Jimmy J.; Ellsworth, Ronald K.; Giron, Rebecca M.; Rood, Jennifer; Bray, George A.; Smith, Steven R.; Wysocki, Vicki H.; Tsao, Tsu‐Shuen

doi:10.1016/j.ab.2013.02.008

Cited by 8 publications

(3 citation statements)

References 68 publications

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“…Immobilizationo ft he receptors (AdipoR1 and AdipoR2)l ed to an increase in R ct of about 5.8 kW,o wing to itsl arge size and probablen eutral charge, [19] making electron diffusion through the biosensor layers difficult. The binding of adiponectin (0.1 mmol l À1 ), which is negatively charged at biological pH, [20] (pI 5.42 [21] ), also increased the R ct value by at least 19 kW,a se xpected, indicatingt he formation of ab locking layer on the surface caused by an adiponectin-specific interaction with itsr eceptors (Figure 1, bottom). The major differenceb etween the signals, before and after adiponectin binding, shows that this architecture is adequate for the adiponectin biosensor.…”

Section: Electrodem Odification-biosensor Fabricationmentioning

confidence: 99%

Transmembrane Protein‐Based Electrochemical Biosensor for Adiponectin Hormone Quantification

et al. 2016

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Decreased adiponectin hormone secretion occurs 10–20 years before chronic hyperglycemia, and is a great indicator of further development of type 2 diabetes. Here, we developed an electrochemical biosensor for adiponectin quantification based on specific transmembrane receptors (AdipoR1 and AdipoR2). Under optimized conditions, cyclic‐voltammetry‐based adiponectin biosensors displayed linearity (R2=0.992) in a wide range of concentrations (0.025–0.75 μmol l−1), including typical human serum levels, with a detection limit of 7.0 nmol L−1 and reproducibility of 1.7 %, n=3. Electrochemical impedance spectroscopy results showed a similar behavior, with a linear increase in charge‐transfer resistance (R2=0.971) from 0.025 to 1.00 μmol l−1, a detection limit of 7.0 nmol L−1, and reproducibility of 5.6 %, n=3. Furthermore, the analytical results obtained by using the biosensor in human serum samples were in agreement with those obtained by using the enzyme‐linked immunosorbent assay (ELISA) at a 95 % confidence level. It is expected the proposed device increases the number of predictive type 2 diabetes diagnostics, promoting early treatment and patient awareness about the precautions to be taken.

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Section: Electrodem Odification-biosensor Fabricationmentioning

confidence: 99%

Transmembrane Protein‐Based Electrochemical Biosensor for Adiponectin Hormone Quantification

et al. 2016

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“…One possible extension of the chemical dynamics simulations are atomistic studies of SID of noncovalent complexes − and additional simulations of peptide SID, with different organic surfaces. Wysocki and co-workers have performed a number of experiments of oligopeptide SID .…”

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confidence: 99%

Dynamics of Protonated Peptide Ion Collisions with Organic Surfaces: Consonance of Simulation and Experiment

Pratihar

Barnes

Laskin

et al. 2016

J. Phys. Chem. Lett.

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In this Perspective, mass spectrometry experiments and chemical dynamics simulations are described that have explored the atomistic dynamics of protonated peptide ions, peptide-H(+), colliding with organic surfaces. These studies have investigated the energy transfer and fragmentation dynamics for peptide-H(+) surface-induced dissociation (SID), peptide-H(+) physisorption on the surface, soft landing (SL), and peptide-H(+) reaction with the surface, reactive landing (RL). SID provides primary structures of biological ions and information regarding their fragmentation pathways and energetics. Two SID mechanisms are found for peptide-H(+) fragmentation. A traditional mechanism in which peptide-H(+) is vibrationally excited by its collision with the surface, rebounds off the surface and then dissociates in accord with the statistical, RRKM unimolecular rate theory. The other, shattering, is a nonstatistical mechanism in which peptide-H(+) fragments as it collides with the surface, dissociating via many pathways and forming many product ions. Shattering is important for collisions with diamond and perfluorinated self-assembled monolayer (F-SAM) surfaces, increasing in importance with the peptide-H(+) collision energy. Chemical dynamics simulations also provide important mechanistic insights on SL and RL of biological ions on surfaces. The simulations indicate that SL occurs via multiple mechanisms consisting of sequences of peptide-H(+) physisorption on and penetration in the surface. SL and RL have a broad range of important applications including preparation of protein or peptide microarrays, development of biocompatible substrates and biosensors, and preparation of novel synthetic materials, including nanomaterials. An important RL mechanism is intact deposition of peptide-H(+) on the surface.

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“…). In plasma, HMW adiponectin has been found as a mixture consisting of nonamer, dodecamer and octadecamer forms with the latter representing the most abundant of these components . Moreover, it has been reported that the hexamer of adiponectin is broken into trimers by treatment with a reducing agent, but the octadecamer of adiponectin is resistant to this .…”

Section: Resultsmentioning

confidence: 99%

Ordered self‐assembly of the collagenous domain of adiponectin with noncovalent interactions via glycosylated lysine residues

et al. 2016

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Edited by Laszlo NagyAdiponectin, an anti-atherogenic and insulin-sensitizing adipokine, forms multiple isoforms including a trimer, a hexamer and heavier oligomers (mainly octadecamer) that determine their biological activities. We designed 89-residue peptides containing modifications found in the collagenous domain of native adiponectin. Circular dichroism and analytical ultracentrifugation measurements showed that the peptide bearing glucosyl-galactosyl-hydroxylysine residues forms a stable collagen-like triple helical structure and spontaneously assembled into an octadecamer. An assembly model mediated by noncovalent interactions via glycosylated lysine residues for the octadecamer was constructed. Our findings clarified an essential role of glycosyl modifications to coordinate the ordered self-assembly of adiponectin.

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High-resolution identification of human adiponectin oligomers and regulation by pioglitazone in type 2 diabetic patients

Cited by 8 publications

References 68 publications

Transmembrane Protein‐Based Electrochemical Biosensor for Adiponectin Hormone Quantification

Transmembrane Protein‐Based Electrochemical Biosensor for Adiponectin Hormone Quantification

Dynamics of Protonated Peptide Ion Collisions with Organic Surfaces: Consonance of Simulation and Experiment

Ordered self‐assembly of the collagenous domain of adiponectin with noncovalent interactions via glycosylated lysine residues

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