Fast screening method for molecular recognition of islet amyloid polypeptide from whole blood samples collected from dia
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RESEARCH PAPER
Fast screening method for molecular recognition of islet amyloid polypeptide from whole blood samples collected from diabetic patients with disposable stochastic sensors obtained by nanolayer, and nanolayer by nanolayer deposition using cold plasma Raluca-Ioana Stefan-van Staden 1 & Ioana Popa-Tudor 1 & Marius Badulescu 2 & Alexandru Anghel 2 Received: 7 March 2020 / Revised: 1 April 2020 / Accepted: 4 April 2020 # Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Nanolayer and nanolayer by nanolayer deposition of nanofilms of Ag and C using cold plasma in sequences (Ag, Ag-C, Ag-AgC), on porous paper, were used to design three disposable stochastic sensors for the assay of amyloid polypeptide from whole blood. The nanofilms were modified with α-cyclodextrin. The test developed using the nanofilm-based disposable stochastic sensors is used for early detection of diabetes. The wider linear concentration range (1.00 × 10−6–1.00 ng mL−1) and the lower limit of quantification (1.00 × 10−6ng mL−1) were obtained using the disposable stochastic sensors based on Ag-C and Ag-Ag-C, while the highest sensitivity (3.19 × 104 s−1/μg mL−1) was recorded using the disposable stochastic sensor based on Ag-Ag-C. The screening methods were fully validated using whole blood samples from confirmed patients, when the recovery of the islet amyloid polypeptide was higher than 98.00%. Keywords IAPP . Stochastic sensors . Diabetes . Whole blood samples
Introduction Diabetes is one of the most common pathologies found worldwide [1]. The storage of amyloid, derived from IAPP (the amyloid polypeptide of the polypeptide hormone islands, also known as amylin), is considered to be the simplest typical modification in type 2 diabetes, this process being known as a hyalinization of the Langerhans islands. Initially, it was not known that amyloid from the island is produced by a polypeptide hormone [2, 3], but subsequently interest in determining IAPP began to increase. Dedicated to Professor Hassan Y. Aboul-Enein on his 75th Birthday. * Raluca-Ioana Stefan-van Staden [email protected] * Marius Badulescu [email protected] 1
Laboratory of Electrochemistry and PATLAB, National Institute of Research for Electrochemistry and Condensed Matter, 202 Splaiul Independenţei Str., 060021 Bucharest-6, Romania
2
National Institute for Laser, Plasma & Radiation Physics, 409 Str Atomistilor, 077125 Măgurele, Romania
In 1938, the first investigations of amyloid from the island were performed [4] and it was observed that it was different from the systemic one. This fact is also evidenced by histochemical studies [5]. The amyloid from the islands was found to be strictly limited to about one million islands representing 1% of the total mass of the pancreas, purified and solubilized in concentrated formic acid solution. After several years of research, a new approach was adopted by identifying the Ab protein [6], using a new purification method by using HPLC (high-performance liquid chromatography). Thus, a new
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