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'''Surface-enhanced laser desorption/ionization''' (SELDI) is a soft [[ionization]] method in [[mass spectrometry]] used for the analysis of [[protein]] [[mixture]]s.<ref name=":0">{{cite journal |author=Tang N, Tornatore P, Weinberger SR |title=Current developments in SELDI affinity technology |journal=Mass spectrometry reviews |volume=23 |issue=1 |pages=34–44 |year=2004 |pmid=14625891 |doi=10.1002/mas.10066}}</ref> SELDI is typically used with [[time-of-flight mass spectrometry|time-of-flight]] (TOF) mass spectrometers and is used to detect proteins in tissue samples, [[blood]], [[urine]], or other clinical samples. Comparison of protein levels between patients with and without a disease can be used for [[biomarker discovery]].<ref>{{cite journal |author=Li J, Zhang Z, Rosenzweig J, Wang YY, Chan DW |title=Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer |journal=Clin. Chem. |volume=48 |issue=8 |pages=1296–304 |year=2002 |pmid=12142387}}</ref><ref>{{cite journal |author=Jr GW, Cazares LH, Leung SM, Nasim S, Adam BL, Yip TT, Schellhammer PF, Gong L, Vlahou A |title=Proteinchip(R) surface enhanced laser desorption/ionization (SELDI) mass spectrometry: a novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures |journal= Prostate Cancer and Prostatic Diseases|volume=2 |issue=5/6 |pages=264–276 |year=1999 |pmid=12497173 |doi=10.1038/sj.pcan.4500384}}</ref> |
'''Surface-enhanced laser desorption/ionization''' (SELDI) is a soft [[ionization]] method in [[mass spectrometry]] used for the analysis of [[protein]] [[mixture]]s.<ref name=":0">{{cite journal |author=Tang N, Tornatore P, Weinberger SR |title=Current developments in SELDI affinity technology |journal=Mass spectrometry reviews |volume=23 |issue=1 |pages=34–44 |year=2004 |pmid=14625891 |doi=10.1002/mas.10066}}</ref> SELDI is typically used with [[time-of-flight mass spectrometry|time-of-flight]] (TOF) mass spectrometers and is used to detect proteins in tissue samples, [[blood]], [[urine]], or other clinical samples. Comparison of protein levels between patients with and without a disease can be used for [[biomarker discovery]].<ref>{{cite journal |author=Li J, Zhang Z, Rosenzweig J, Wang YY, Chan DW |title=Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer |journal=Clin. Chem. |volume=48 |issue=8 |pages=1296–304 |year=2002 |pmid=12142387}}</ref><ref>{{cite journal |author=Jr GW, Cazares LH, Leung SM, Nasim S, Adam BL, Yip TT, Schellhammer PF, Gong L, Vlahou A |title=Proteinchip(R) surface enhanced laser desorption/ionization (SELDI) mass spectrometry: a novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures |journal= Prostate Cancer and Prostatic Diseases|volume=2 |issue=5/6 |pages=264–276 |year=1999 |pmid=12497173 |doi=10.1038/sj.pcan.4500384}}</ref> |
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== History == |
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| ⚫ | SELDI technology was developed by T. William Hutchens and Tai-Tung Yip at [[Baylor College of Medicine]] in 1993.<ref>Hutchens TW and Yip TT. "New desorption strategies for the mass spectrometric analysis of macromolecules." Rapid Commun Mass Spectrom 7: 576-580 (1993). [http://dx.doi.org/10.1002/rcm.1290070703]</ref> The technology was first commercialized by Ciphergen Biosystems in 1997 as the ProteinChip system, and is now produced and marketed by [[Bio-Rad]] Laboratories.<ref>{{Cite book|url=http://onlinelibrary.wiley.com/doi/10.1002/9780470061565.hbb128/abstract|title=Surface-Enhanced Laser Desorption/Ionization (SELDI) Technology|last=Lomas|first=Lee O.|last2=Weinberger|first2=Scot R.|date=2008-01-01|publisher=John Wiley & Sons, Ltd|isbn=9780470061565|language=en|doi=10.1002/9780470061565.hbb128}}</ref> |
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== Fundamentals == |
== Fundamentals == |
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Binding to the SELDI surface acts as a separation step, and as a result, the proteins bound to the surface are easier to analyze. The surface is composed primarily of materials with a variety of physico-chemical characteristics, metal ions, or anion or cation exchangers. Common surfaces include CM10 (weak cation [[Ion exchange|exchange]]), H50 (hydrophobic surface, similar to C<sub>6</sub>-C<sub>12</sub> [[reverse phase chromatography]]), IMAC30 (metal-binding surface), and Q10 (strong anion exchange). SELDI surfaces can also be functionalized to study DNA-protein binding, antibody-antigen assays, and receptor-ligand interactions.<ref name=":1" /> |
Binding to the SELDI surface acts as a separation step, and as a result, the proteins bound to the surface are easier to analyze. The surface is composed primarily of materials with a variety of physico-chemical characteristics, metal ions, or anion or cation exchangers. Common surfaces include CM10 (weak cation [[Ion exchange|exchange]]), H50 (hydrophobic surface, similar to C<sub>6</sub>-C<sub>12</sub> [[reverse phase chromatography]]), IMAC30 (metal-binding surface), and Q10 (strong anion exchange). SELDI surfaces can also be functionalized to study DNA-protein binding, antibody-antigen assays, and receptor-ligand interactions.<ref name=":1" /> |
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==Commercialization== |
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| ⚫ | SELDI technology was developed by T. William Hutchens at [[Baylor College of Medicine]] in 1993.<ref>Hutchens TW and Yip TT. "New desorption strategies for the mass spectrometric analysis of macromolecules." Rapid Commun Mass Spectrom 7: 576-580 (1993). [http://dx.doi.org/10.1002/rcm.1290070703]</ref> The technology was commercialized by |
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==See also== |
==See also== |
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Revision as of 09:29, 27 March 2016
| Acronym | SELDI |
|---|---|
| Analytes | Biomolecules |
| Other techniques | |
| Related | Matrix-assisted laser desorption/ionization Soft laser desorption Surface-assisted laser desorption/ionization |
Surface-enhanced laser desorption/ionization (SELDI) is a soft ionization method in mass spectrometry used for the analysis of protein mixtures.[1] SELDI is typically used with time-of-flight (TOF) mass spectrometers and is used to detect proteins in tissue samples, blood, urine, or other clinical samples. Comparison of protein levels between patients with and without a disease can be used for biomarker discovery.[2][3]
History
SELDI technology was developed by T. William Hutchens and Tai-Tung Yip at Baylor College of Medicine in 1993.[4] The technology was first commercialized by Ciphergen Biosystems in 1997 as the ProteinChip system, and is now produced and marketed by Bio-Rad Laboratories.[5]
Fundamentals
SELDI is a variation of matrix-assisted laser desorption/ionization (MALDI) and incorporates surface-enhanced neat desorption (SEND) and surface-enhanced affinity-capture (SEAC) mass spectrometry.[1]
A major advantage of the SELDI process is that sample components that interfere with other analytical tools, including salts, detergents, buffers, or other compounds, are removed before analysis with mass spectrometry. Only the proteins that are specifically bound to the spot surfaces are analyzed, reducing the overall complexity of the sample. As a result, there is an increased probability of detecting analytes that are present in lower concentrations.[6]
Sample Preparation & Instrumentation
SELDI can be seen as a combination of solid-phase chromatography and TOF-MS. The sample is spotted onto a modified chip surface, where each spot on the surface allows for the specific binding of proteins from the sample. Contaminants and nonspecifically bound proteins are then washed away. After washing the spotted sample, an energy absorbing matrix is applied to the surface and allowed to crystallize with the sample. The sample is then irradiated by a pulsed laser, causing ablation and desorption of the sample and matrix.[1][7]
Samples spotted on a SELDI surface are typically analyzed using time-of-flight mass spectrometry. A laser ionizes peptides from crystals of the sample/matrix mixture. The ions are accelerated through an electric potential and down a flight tube. A detector measures ions as they reach the end of the tube. The mass-to-charge ratio of each ion can be determined from the length of the tube, the kinetic energy given to ions by the electric field, and the time taken to travel the length of the tube.
Binding to the SELDI surface acts as a separation step, and as a result, the proteins bound to the surface are easier to analyze. The surface is composed primarily of materials with a variety of physico-chemical characteristics, metal ions, or anion or cation exchangers. Common surfaces include CM10 (weak cation exchange), H50 (hydrophobic surface, similar to C6-C12 reverse phase chromatography), IMAC30 (metal-binding surface), and Q10 (strong anion exchange). SELDI surfaces can also be functionalized to study DNA-protein binding, antibody-antigen assays, and receptor-ligand interactions.[7]
See also
References
- ^ a b c Tang N, Tornatore P, Weinberger SR (2004). "Current developments in SELDI affinity technology". Mass spectrometry reviews. 23 (1): 34–44. doi:10.1002/mas.10066. PMID 14625891.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Li J, Zhang Z, Rosenzweig J, Wang YY, Chan DW (2002). "Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer". Clin. Chem. 48 (8): 1296–304. PMID 12142387.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Jr GW, Cazares LH, Leung SM, Nasim S, Adam BL, Yip TT, Schellhammer PF, Gong L, Vlahou A (1999). "Proteinchip(R) surface enhanced laser desorption/ionization (SELDI) mass spectrometry: a novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures". Prostate Cancer and Prostatic Diseases. 2 (5/6): 264–276. doi:10.1038/sj.pcan.4500384. PMID 12497173.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Hutchens TW and Yip TT. "New desorption strategies for the mass spectrometric analysis of macromolecules." Rapid Commun Mass Spectrom 7: 576-580 (1993). [1]
- ^ Lomas, Lee O.; Weinberger, Scot R. (2008-01-01). Surface-Enhanced Laser Desorption/Ionization (SELDI) Technology. John Wiley & Sons, Ltd. doi:10.1002/9780470061565.hbb128. ISBN 9780470061565.
- ^ Seibert, Volker; Wiesner, Andreas; Buschmann, Thomas; Meuer, Jörn (2004-04-30). "Surface-enhanced laser desorption ionization time-of-flight mass spectrometry (SELDI TOF-MS) and ProteinChip® technology in proteomics research". Pathology - Research and Practice. Proteomics in Pathology, Research and Practice. 200 (2): 83–94. doi:10.1016/j.prp.2004.01.010.
- ^ a b Muthu, Manikandan; Vimala, A.; Mendoza, Ordetta Hanna; Gopal, Judy (2016-02-01). "Tracing the voyage of SELDI-TOF MS in cancer biomarker discovery and its current depreciation trend – need for resurrection?". TrAC Trends in Analytical Chemistry. 76: 95–101. doi:10.1016/j.trac.2015.10.004.