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Glycated albumin precipitation using aptamer conjugated magnetic nanoparticles.
Sci Rep. 2020 Jul 01; 10(1):10716.SR

Abstract

To develop a strategy for the elimination of prefibrillar amyloid aggregates, a three-step non-modified DNA aptamer conjugation on silica-coated magnetic nanoparticles was carried out to achieve aptamer conjugated on MNP (Ap-SiMNP). Prefibrillar amyloid aggregates are generated under a diabetic condition which are prominently participated in developing diabetic complications. The binding properties of candidate DNA aptamer against serum albumin prefibrillar amyloid aggregates (AA20) were verified using electrophoretic mobility shift assay (EMSA) and surface plasmon resonance spectroscopy (SPR) analysis. The chloro-functionalized silica-coated MNPs were synthesized then a nano-targeting structure as aptamer conjugated on MNP (Ap-SiMNP) was constructed. Finally, Ap-SiMNP was verified for specific binding efficiency and AA20 removal using an external magnetic field. The candidate aptamer showed a high binding capacity at EMSA and SPR analysis (KD = 3.4 × 10─9 M) and successfully used to construct Ap-SiMNP. Here, we show a proof of concept for an efficient bio-scavenger as Ap-SiMNP to provide a promising opportunity to consider as a possible strategy to overcome some diabetic complications through specific binding/removal of toxic AA20 species.

Authors+Show Affiliations

School of Biology, University of Tehran, P.O.Box 14155-6455, Tehran, Iran.School of Biology, University of Tehran, P.O.Box 14155-6455, Tehran, Iran. mhabibi@ut.ac.ir. Center of Excellence in Nano-Biomedicine, University of Tehran, Tehran, Iran. mhabibi@ut.ac.ir.Research Center for Gastroenterology and Liver Disease, Baqiyatallah University of Medical Sciences, Tehran, Iran.Department of Cell and Molecular Biology and Microbiology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran.Nanobiotechnolology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32612182

Citation

Fayazi, R, et al. "Glycated Albumin Precipitation Using Aptamer Conjugated Magnetic Nanoparticles." Scientific Reports, vol. 10, no. 1, 2020, p. 10716.
Fayazi R, Habibi-Rezaei M, Heiat M, et al. Glycated albumin precipitation using aptamer conjugated magnetic nanoparticles. Sci Rep. 2020;10(1):10716.
Fayazi, R., Habibi-Rezaei, M., Heiat, M., Javadi-Zarnaghi, F., & Taheri, R. A. (2020). Glycated albumin precipitation using aptamer conjugated magnetic nanoparticles. Scientific Reports, 10(1), 10716. https://doi.org/10.1038/s41598-020-67469-6
Fayazi R, et al. Glycated Albumin Precipitation Using Aptamer Conjugated Magnetic Nanoparticles. Sci Rep. 2020 Jul 1;10(1):10716. PubMed PMID: 32612182.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Glycated albumin precipitation using aptamer conjugated magnetic nanoparticles. AU - Fayazi,R, AU - Habibi-Rezaei,M, AU - Heiat,M, AU - Javadi-Zarnaghi,F, AU - Taheri,R A, Y1 - 2020/07/01/ PY - 2019/09/28/received PY - 2020/06/02/accepted PY - 2020/7/3/entrez PY - 2020/7/3/pubmed PY - 2020/7/3/medline SP - 10716 EP - 10716 JF - Scientific reports JO - Sci Rep VL - 10 IS - 1 N2 - To develop a strategy for the elimination of prefibrillar amyloid aggregates, a three-step non-modified DNA aptamer conjugation on silica-coated magnetic nanoparticles was carried out to achieve aptamer conjugated on MNP (Ap-SiMNP). Prefibrillar amyloid aggregates are generated under a diabetic condition which are prominently participated in developing diabetic complications. The binding properties of candidate DNA aptamer against serum albumin prefibrillar amyloid aggregates (AA20) were verified using electrophoretic mobility shift assay (EMSA) and surface plasmon resonance spectroscopy (SPR) analysis. The chloro-functionalized silica-coated MNPs were synthesized then a nano-targeting structure as aptamer conjugated on MNP (Ap-SiMNP) was constructed. Finally, Ap-SiMNP was verified for specific binding efficiency and AA20 removal using an external magnetic field. The candidate aptamer showed a high binding capacity at EMSA and SPR analysis (KD = 3.4 × 10─9 M) and successfully used to construct Ap-SiMNP. Here, we show a proof of concept for an efficient bio-scavenger as Ap-SiMNP to provide a promising opportunity to consider as a possible strategy to overcome some diabetic complications through specific binding/removal of toxic AA20 species. SN - 2045-2322 UR - https://www.unboundmedicine.com/medline/citation/32612182/Glycated_albumin_precipitation_using_aptamer_conjugated_magnetic_nanoparticles L2 - http://dx.doi.org/10.1038/s41598-020-67469-6 DB - PRIME DP - Unbound Medicine ER -
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