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      Aptasensors versus immunosensors—Which will prevail?

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          Abstract

          Since the invention of the first biosensors 70 years ago, they have turned into valuable and versatile tools for various applications, ranging from disease diagnosis to environmental monitoring. Traditionally, antibodies have been employed as the capture probes in most biosensors, owing to their innate ability to bind their target with high affinity and specificity, and are still considered as the gold standard. Yet, the resulting immunosensors often suffer from considerable limitations, which are mainly ascribed to the antibody size, conjugation chemistry, stability, and costs. Over the past decade, aptamers have emerged as promising alternative capture probes presenting some advantages over existing constraints of immunosensors, as well as new biosensing concepts. Herein, we review the employment of antibodies and aptamers as capture probes in biosensing platforms, addressing the main aspects of biosensor design and mechanism. We also aim to compare both capture probe classes from theoretical and experimental perspectives. Yet, we highlight that such comparisons are not straightforward, and these two families of capture probes should not be necessarily perceived as competing but rather as complementary. We, thus, elaborate on their combined use in hybrid biosensing schemes benefiting from the advantages of each biorecognition element.

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          Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase

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            In vitro selection of RNA molecules that bind specific ligands.

            Subpopulations of RNA molecules that bind specifically to a variety of organic dyes have been isolated from a population of random sequence RNA molecules. Roughly one in 10(10) random sequence RNA molecules folds in such a way as to create a specific binding site for small ligands.
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              Aptamer-Based Multiplexed Proteomic Technology for Biomarker Discovery

              Background The interrogation of proteomes (“proteomics”) in a highly multiplexed and efficient manner remains a coveted and challenging goal in biology and medicine. Methodology/Principal Findings We present a new aptamer-based proteomic technology for biomarker discovery capable of simultaneously measuring thousands of proteins from small sample volumes (15 µL of serum or plasma). Our current assay measures 813 proteins with low limits of detection (1 pM median), 7 logs of overall dynamic range (∼100 fM–1 µM), and 5% median coefficient of variation. This technology is enabled by a new generation of aptamers that contain chemically modified nucleotides, which greatly expand the physicochemical diversity of the large randomized nucleic acid libraries from which the aptamers are selected. Proteins in complex matrices such as plasma are measured with a process that transforms a signature of protein concentrations into a corresponding signature of DNA aptamer concentrations, which is quantified on a DNA microarray. Our assay takes advantage of the dual nature of aptamers as both folded protein-binding entities with defined shapes and unique nucleotide sequences recognizable by specific hybridization probes. To demonstrate the utility of our proteomics biomarker discovery technology, we applied it to a clinical study of chronic kidney disease (CKD). We identified two well known CKD biomarkers as well as an additional 58 potential CKD biomarkers. These results demonstrate the potential utility of our technology to rapidly discover unique protein signatures characteristic of various disease states. Conclusions/Significance We describe a versatile and powerful tool that allows large-scale comparison of proteome profiles among discrete populations. This unbiased and highly multiplexed search engine will enable the discovery of novel biomarkers in a manner that is unencumbered by our incomplete knowledge of biology, thereby helping to advance the next generation of evidence-based medicine.
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                Author and article information

                Contributors
                esegal@technion.ac.il
                Journal
                Eng Life Sci
                Eng Life Sci
                10.1002/(ISSN)1618-2863
                ELSC
                Engineering in Life Sciences
                John Wiley and Sons Inc. (Hoboken )
                1618-0240
                1618-2863
                13 January 2022
                March 2022
                : 22
                : 3-4 , Dedicated to Professor Thomas Scheper ( doiID: 10.1002/elsc.v22.3-4 )
                : 319-333
                Affiliations
                [ 1 ] Faculty of Biotechnology and Food Engineering Technion ‐ Israel Institute of Technology Haifa Israel
                [ 2 ] Institute of Technical Chemistry Leibniz University Hannover Hannover Germany
                [ 3 ] Russell Berrie Nanotechnology Institute Technion ‐ Israel Institute of Technology Haifa Israel
                Author notes
                [*] [* ] Correspondence

                Ester Segal, Faculty of Biotechnology and Food Engineering, Technion ‐ Israel Institute of Technology, Haifa 3200003, Israel.

                Email: esegal@ 123456technion.ac.il

                Author information
                https://orcid.org/0000-0002-3694-0008
                https://orcid.org/0000-0001-9472-754X
                Article
                ELSC1467
                10.1002/elsc.202100148
                8961048
                35382545
                a7a03be0-25b5-4413-b7c0-3c3ae66a928d
                © 2022 The Authors. Engineering in Life Sciences published by Wiley‐VCH GmbH

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 21 December 2021
                : 22 November 2021
                : 24 December 2021
                Page count
                Figures: 4, Tables: 0, Pages: 15, Words: 9893
                Funding
                Funded by: German Research Foundation , doi 10.13039/501100001659;
                Award ID: SCHE 279/32‐1
                Categories
                Review
                Review
                Custom metadata
                2.0
                March 2022
                Converter:WILEY_ML3GV2_TO_JATSPMC version:6.1.2 mode:remove_FC converted:29.03.2022

                antibody,antibody‐aptamer hybrid,aptamer,biosensors,capture probes

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