Because of the inherent complexity of biochemical pathways commonly altered in disease states, it has become accepted that multiplexed analyses can provide a more informative biomolecular understanding of disease onset and progression. Importantly, compared to conventional single-parameter assays, the detailed biomolecular insight gleaned from multiparameter measurements has the potential to greatly improve disease diagnostics, prognostics, and theragnostics. We have previously reported the utility of silicon photonic microring resonators for the sensitive quantitation of a single disease biomarker and herein demonstrate the first example of optical microcavity resonator arrays performing quantitative, label-free, multiplexed analyses of clinically relevant protein biomarkers. In this report, the concentrations of prostate specific antigen (PSA), alpha-fetoprotein (AFP), carcinoembryonic antigen (CEA), tumor necrosis factor-alpha (TNF-alpha), and interleukin-8 (IL-8) are simultaneously determined in three unknown protein cocktail solutions. This letter demonstrates that multiple immunoassays can be performed concurrently on a microresonator platform without any accompanying loss of sensitivity or measurement precision, and therefore, this report lays the groundwork for future applications involving multiplexed analysis of clinically relevant samples.
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http://dx.doi.org/10.1021/ac902451b | DOI Listing |
Adv Healthc Mater
December 2024
Department of Mechanical Engineering, Johns Hopkins University, Baltimore, MD, 21218, USA.
Astrocytes, integral components of the central nervous system, are increasingly recognized for their multifaceted roles beyond support cells. Despite their acknowledged importance, understanding the intricacies of astrocyte morphological dynamics remains limited. Our study marks the first exploration of astrocytes using optical diffraction tomography (ODT), establishing a label-free, quantitative method to observe morphological changes in astrocytes over a 7-day in-vitro period.
View Article and Find Full Text PDFSci Rep
December 2024
Neurobiology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Proximity-dependent biotinylation coupled with mass spectrometry enables the characterization of subcellular proteomes. This technique has significantly advanced neuroscience by revealing sub-synaptic protein networks, such as the synaptic cleft and post-synaptic density. Profiling proteins at this detailed level is essential for understanding the molecular mechanisms of neuronal connectivity and transmission.
View Article and Find Full Text PDFAdv Mater
December 2024
Advanced Microscopy and Instrumentation Research Center, School of Instrumentation Science and Engineering, Harbin Institute of Technology, Harbin, 150080, China.
In this paper, compact terahertz (THz) metachips for hyperspectral screening and quantitative evaluation of human cancer cells is reported. This pixelated resonant metachips feature the resonance channel from 1 and 3 THz frequency with a record-high quality factor (up to 230). Through the interactions of various cancer cells of different concentrations, high-dimensional spectral signatures are obtained, which are further transformed into a spatial map for labelling and quantification purposes.
View Article and Find Full Text PDFFood Chem
December 2024
Chinese Academy of Inspection and Quarantine, Beijing 100176, People's Republic of China. Electronic address:
Glycoproteins, which are involved in numerous biological functions, are among the most critical functional ingredients in an edible bird's nest (EBN). To gain a comprehensive understanding of the glycoprotein species within EBN, a label-free, site-specific glycoproteomic approach was used to analyze their N-glycoproteins, N-glycopeptides, and N-glycans systematically. A total of 127 N-glycoproteins were identified in EBN, of which 72 were found in house-EBN and 63 in cave-EBN, yielding 4195 and 5649 glycopeptides, respectively.
View Article and Find Full Text PDFPoult Sci
December 2024
Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, No. 2025 Chengluo Avenue, Chengdu 610106, China. Electronic address:
Egg white proteins are widely recognized as excellent natural emulsifiers, yet the molecular mechanisms underlying their emulsification properties remain incompletely understood, particularly regarding the roles of individual proteins in complex natural systems. Using 4D-label-free quantitative proteomics, we systematically investigated protein dynamics during egg white emulsification by comparing egg white (EW) and the aqueous phases of egg white emulsions (EWE-W). Proteomic analysis identified 96 distinct proteins, with 64 showing significant abundance changes during emulsification.
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