Matrix-enhanced nanostructure initiator mass spectrometry (ME-NIMS) for small molecule detection and imaging

2016 ◽  
Vol 8 (46) ◽  
pp. 8234-8240 ◽  
Author(s):  
Tara N. Moening ◽  
Victoria L. Brown ◽  
Lin He

ME-NIMS MS imaging (right): significantly enhanced sensitivity over conventional NIMS (left) in tissue imaging.

2004 ◽  
Vol 808 ◽  
Author(s):  
Grace Credo ◽  
Hillary Hewitson ◽  
Christopher Benevides ◽  
Edouard S. P. Bouvier

ABSTRACTPrevious work has demonstrated the utility of desorption/ionization on silicon (DIOS) time-of-flight mass spectrometry (TOFMS) in drug molecule and peptide detection[1-7]. In this work, the utility of DIOS for small molecule detection is established using commercially available porous silicon (por Si)-based target plates for MS. Since the morphology and handling of the substrates can have dramatic effects on the MS characteristics, the development of consistent manufacturing methods and characterization protocols has been central to the production of reproducible target plates[7]. Using sample substrates manufactured in-house, we show that 1) small molecules and protein digests were detected without matrix-related peaks, 2) por Si morphology was optimized for small molecule detection, 3) reproducible DIOS plates were produced, 4) although the target plates were shown to be sensitive to contamination, a consistent cleaning procedure was developed to remove contaminants, and 5) stability and shelf life were characterized as a function of surface derivatization. Dynamic range, sensitivity, quantitation, speed of analysis, solution composition, and automated deposition have also been evaluated and are described in related work[7-9]. Potential applications include high-throughput small molecule assays for drug discovery[10a] and high sensitivity (sub-femtomole) peptide identification for proteomics[10b].


2019 ◽  
Vol 16 (4) ◽  
pp. 267-276
Author(s):  
Qurat ul Ain Farooq ◽  
Noor ul Haq ◽  
Abdul Aziz ◽  
Sara Aimen ◽  
Muhammad Inam ul Haq

Background: Mass spectrometry is a tool used in analytical chemistry to identify components in a chemical compound and it is of tremendous importance in the field of biology for high throughput analysis of biomolecules, among which protein is of great interest. Objective: Advancement in proteomics based on mass spectrometry has led the way to quantify multiple protein complexes, and proteins interactions with DNA/RNA or other chemical compounds which is a breakthrough in the field of bioinformatics. Methods: Many new technologies have been introduced in electrospray ionization (ESI) and Matrixassisted Laser Desorption/Ionization (MALDI) techniques which have enhanced sensitivity, resolution and many other key features for the characterization of proteins. Results: The advent of ambient mass spectrometry and its different versions like Desorption Electrospray Ionization (DESI), DART and ELDI has brought a huge revolution in proteomics research. Different imaging techniques are also introduced in MS to map proteins and other significant biomolecules. These drastic developments have paved the way to analyze large proteins of >200kDa easily. Conclusion: Here, we discuss the recent advancement in mass spectrometry, which is of great importance and it could lead us to further deep analysis of the molecules from different perspectives and further advancement in these techniques will enable us to find better ways for prediction of molecules and their behavioral properties.


2008 ◽  
Vol 120 (49) ◽  
pp. 9660-9663 ◽  
Author(s):  
Jung Rok Lee ◽  
Juhee Lee ◽  
Sang Kyung Kim ◽  
Kwang Pyo Kim ◽  
Hyung Soon Park ◽  
...  

2020 ◽  
Author(s):  
Rhushabh Maugi ◽  
bernadette gamble ◽  
david bunka ◽  
Mark Platt

A universal aptamer-based sensing strategy is proposed using DNA modified nanocarriers and Resistive Pulse Sensing for the rapid and label free detection of small molecules. The surface of a magnetic nanocarrier was first modified with a ssDNA aka linker which is designed to be partially complimentary in sequence to a ssDNA aptamer. The aptamer and linker form a stable dsDNA complex on the nanocarriers surface. Upon the addition of the target molecule, a conformational change takes place where the aptamer preferentially binds to the target over the linker; causing the aptamer to be released into solution. The RPS measures the change in velocity of the nanocarrier as its surface changes from dsDNA to ssDNA, and its velocity is used as a proxy for the concentration of the target. We illustrate the versatility of the assay by demonstrating the detection of the antibiotic Moxifloxacin, and chemotherapeutics Imatinib and Irinotecan.


2020 ◽  
Author(s):  
lingpeng zhan ◽  
xi huang ◽  
jinjuan xue ◽  
huihui liu ◽  
caiqiao xiong ◽  
...  

Mass spectrometry imaging (MSI) has been increasingly utilized in investigating the locations of biomolecules within tissues. However, the isomeric compounds are rarely distinguished in the MS images, due to inability of MSI methods to differentiate isomers in the probing area. Coupling tandem mass spectrometry with MSI can facilitate differentiating isomeric compounds in ion images. Here we apply MALDI-TOF/TOF tandem mass spectrometry imaging approach to revealing the spatial distributions of isomeric disaccharides in plant tissues. First, the MS/MS imaging analysis of disaccharide-matrix droplet spots demonstrated the feasibility of distinguishing isomeric species in tissues, by measuring the relative intensity of specific fragments. Then, we conducted tandem MS imaging of disaccharides in onion bulb tissues, which indicated that sucrose and other unknown non-sucrose disaccharides exhibit heterogeneous locations throughout the tissues. This method enables us to image disaccharide isomers differentially in biological tissues, and to discover new saccharide species in plant. This work also emphasizes the necessity of considering isobaric compounds when interpreting MSI results.<br>


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