Surface Plasmon Resonance-Laser Desorption/Ionization-Time-of-Flight Mass Spectrometry

Owega, Sandy; Lai, Edward P. C.; Bawagan, A.D.O.

doi:10.1021/ac971166u

Cited by 24 publications

(18 citation statements)

References 16 publications

(19 reference statements)

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“…The signal depends on the morphology of the sample being irradiated. Efforts to avoid the use of an organic matrix include excitation under surface plasmon resonance conditions (20) and the use of porous silicon as a substrate (21).…”

Section: Maldi and Electrospraymentioning

confidence: 99%

Peptides and Proteins in the Vapor Phase

Jarrold

2000

Annu. Rev. Phys. Chem.

346

341

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This article provides a review of recent studies of the properties of unsolvated (and partially solvated) peptides and proteins. The methods used to produce vapor-phase peptide and protein ions are described along with some of the techniques used to study them, such as H/D exchange, blackbody infrared radiative dissociation, and ion mobility measurements. Studies of unsolvated peptides and proteins provide information about their intrinsic intramolecular interactions. The topics covered include the role of zwitterions and salt bridges in the vapor phase, Coulomb interactions in multiply charged ions, the unfolding and refolding of vapor-phase proteins, and the stability of unsolvated helices and sheets. Finally, dehydration and rehydration studies of proteins in the vapor phase are described. These can provide exquisitely detailed information about hydration interactions, such as the enthalpy and entropy changes associated with adsorbing individual water molecules.

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Section: Maldi and Electrospraymentioning

confidence: 99%

Peptides and Proteins in the Vapor Phase

Jarrold

2000

Annu. Rev. Phys. Chem.

346

341

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“…Therefore, MALDI-TOF allows to identify the molecule(s) from the mixture that interact with the sensor [53,54]. The combination is very efficient because the metal layer concurs in the laser desorption/ionization process [55]. The direct application of MALDI-TOF on the sensor chip is however destructive.…”

Section: Biomedical Applications Of Spr With Biosensorsmentioning

confidence: 99%

Surface plasmon resonance: principles, methods and applications in biomedical sciences

Englebienne

Hoonacker

Verhas

2003

Journal of Spectroscopy

293

140

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Surface plasmon resonance (SPR) is a phenomenon occuring at metal surfaces (typically gold and silver) when an incident light beam strikes the surface at a particular angle. Depending on the thickness of a molecular layer at the metal surface, the SPR phenomenon results in a graded reduction in intensity of the reflected light. Biomedical applications take advantage of the exquisite sensitivity of SPR to the refractive index of the medium next to the metal surface, which makes it possible to measure accurately the adsorption of molecules on the metal surface and their eventual interactions with specific ligands. The last ten years have seen a tremendous development of SPR use in biomedical applications. The technique is applied not only to the measurement in real-time of the kinetics of ligand–receptor interactions and to the screening of lead compounds in the pharmaceutical industry, but also to the measurement of DNA hybridization, enzyme–substrate interactions, in polyclonal antibody characterization, epitope mapping, protein conformation studies and label-free immunoassays. Conventional SPR is applied in specialized biosensing instruments. These instruments use expensive sensor chips of limited reuse capacity and require complex chemistry for ligand or protein immobilization. Our laboratory has successfully applied SPR with colloidal gold particles in buffered solution. This application offers many advantages over conventional SPR. The support is cheap, easily synthesized, and can be coated with various proteins or protein–ligand complexes by charge adsorption. With colloidal gold, the SPR phenomenon can be monitored in any UV-vis spectrophotometer. For high‒throughput applications, we have adapted the technology in an automated clinical chemistry analyzer. This simple technology finds application in label-free quantitative immunoassay techniques for proteins and small analytes, in conformational studies with proteins as well as in the real-time association-dissociation measurements of receptor–ligand interactions, for high-throughput screening and lead optimization.

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“…Common sample targets are stainless steel, but more exotic materials can also be used as they are particularly useful in the combination of MALDI and other analytical methods, e.g. with surface plasmon resonance ([52,53]) or with polyacrylamide gel electrophoresis (PAGE; [54–56]). Alternatively, the application of polymeric coatings to sample targets can be used to improve MALDI performance (see, e.g., [57,58]).…”

Section: Ms Methodsmentioning

confidence: 99%

Characterisation of bacteria by matrix-assisted laser desorption/ionisation and electrospray mass spectrometry

Baar¹

2000

FEMS Microbiology Reviews

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Chemical analysis for the characterisation of micro‐organisms is rapidly evolving, after the recent advent of new ionisation methods in mass spectrometry (MS): electrospray (ES) and matrix‐assisted laser desorption/ionisation (MALDI). These methods allow quick characterisation of micro‐organisms, either directly or after minimum sample preparation. This review provides a brief introduction to ES and MALDI MS and a discussion of micro‐organism characterisation capabilities. Some attention is devoted to the analysis of mixtures of proteins, lipids and other compounds, to the combination of polymerase chain reaction technology and MS, and to the analysis of whole bacteria and their lysates. The review of results produced hitherto is concluded with an outlook on future developments.

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Surface Plasmon Resonance-Laser Desorption/Ionization-Time-of-Flight Mass Spectrometry

Cited by 24 publications

References 16 publications

Peptides and Proteins in the Vapor Phase

Peptides and Proteins in the Vapor Phase

Surface plasmon resonance: principles, methods and applications in biomedical sciences

Characterisation of bacteria by matrix-assisted laser desorption/ionisation and electrospray mass spectrometry

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