Recent Progress in Development and Application of DNA, Protein, Peptide, Glycan, Antibody, and Aptamer Microarrays

Abstract

Microarrays are one of the trailblazing technologies of the last two decades and have displayed their importance in all the associated fields of biology. They are widely explored to screen, identify, and gain insights on the characteristics traits of biomolecules (individually or in complex solutions). A wide variety of biomolecule-based microarrays (DNA microarrays, protein microarrays, glycan microarrays, antibody microarrays, peptide microarrays, and aptamer microarrays) are either commercially available or fabricated in-house by researchers to explore diverse substrates, surface coating, immobilization techniques, and detection strategies. The aim of this review is to explore the development of biomolecule-based microarray applications since 2018 onwards. Here, we have covered a different array of printing strategies, substrate surface modification, biomolecule immobilization strategies, detection techniques, and biomolecule-based microarray applications. The period of 2018–2022 focused on using biomolecule-based microarrays for the identification of biomarkers, detection of viruses, differentiation of multiple pathogens, etc. A few potential future applications of microarrays could be for personalized medicine, vaccine candidate screening, toxin screening, pathogen identification, and posttranslational modifications.

Proteomics—The State of the Field: The Definition and Analysis of Proteomes Should Be Based in Reality, Not Convenience

“…There has always been a trend in science to adapt technologies from one field to another. Micro-arrays used for transcriptome analysis were adapted to protein arrays, although the technology did not achieve widespread use because of cost and other deficiencies [ 209 , 210 ]. Proteomics is currently seeing adoption of technology from genomics and NGS, where signal output is from amplification of oligonucleotide fragments attached to either antibodies (Olink) or aptamers (Somascan) that bind to a discreet part of a protein molecule, usually a series of amino acids (that could potentially include a PTM) [ 209 , 211 , 212 , 213 ].…”

How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?

“…Table 1 lists major proteomic techniques, as well as a variety of biochemical, immunochemical and cell biological methods that can be used to independently verify the MS-based identification of specific proteoforms or the findings of changes in protein abundance from comparative proteomic studies. These methods are frequently employed to study cell or tissue specimens derived from normal versus diseased skeletal muscles, including the following: Two-dimensional gel electrophoresis (2D-GE) [ 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 71 ]; Differential imaging gel electrophoresis (2D-DIGE) [ 86 , 87 , 88 , 89 , 90 , 91 , 92 , 93 ]; Specialized gel-based methods for studying specific protein species [ 67 , 68 , 69 , 77 , 78 , 79 , 80 ]; Gel electrophoresis–liquid chromatography methods (GeLC) [ 103 , 104 , 105 ]; Protein microarrays [ 143 , 144 , 145 , 146 ]; Sample preparation for proteomic analysis [ 89 , 113 , 114 , …”

Construction of Targeting-Peptide-Based Imaging Reagents and Their Application in Bioimaging

“…Compared to common biorecognition molecules (aptamer, DNA, glycan, antibody, etc. ), targeting peptides, apart from their shared biocompatibility, high selectivity, and specificity, can form richer sequences due to the diversity of amino acids that make up peptides. − Moreover, due to the designability of the targeting peptide, stapled peptides, cyclic peptides, etc., have been developed for molecular recognition scenarios to increase the affinity and stability to the target. , However, during targeting peptide recognition, there exists a special class of targets whose binding interface consists of β-strand-rich structures (e.g., PD-L1 and PD-1, etc.) .…”