BLI-MS: Combining biolayer interferometry and mass spectrometry.
biolayer interferometry
mass spectrometry
molecular interaction
Journal
Proteomics
ISSN: 1615-9861
Titre abrégé: Proteomics
Pays: Germany
ID NLM: 101092707
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
revised:
30
11
2021
received:
03
02
2021
accepted:
20
12
2021
pubmed:
28
12
2021
medline:
6
5
2022
entrez:
27
12
2021
Statut:
ppublish
Résumé
Biolayer interferometry (BLI) is a technology which allows to study the affinity between two interacting macro-molecules and to visualize their kinetic of interaction in real time. In this work, we combine BLI interaction measurement with mass spectrometry in order to identify the proteins interacting with the bait. We provide for the first time the proof of concept of the feasibility of BLI-MS in complex biological mixtures.
Identifiants
pubmed: 34958708
doi: 10.1002/pmic.202100031
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2100031Informations de copyright
© 2022 Wiley-VCH GmbH.
Références
Piliarik, M., Vaisocherová, H., & Homola, J. (2009). In A. Rasooly, & K. E. Herold (Eds.), Biosensors and biodetection: Methods in molecular biology (pp. 65-88). Humana Press.
Altschuh, D., Dubs, M. C., Weiss, E., Zeder-Lutz, G., & Van Regenmortel, M. H. V. (1992). Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance. Biochemistry, 31, 6298-6304.
Malmqvist, M. (1993). Surface plasmon resonance for detection and measurement of antibody-antigen affinity and kinetics. Current Opinion in Immunology, 5, 282-286.
Concepcion, J., Witte, K., Wartchow, C., Choo, S., Yao, D., Persson, H., Wei, J., Li, P., Heidecker, B., Ma, W., Varma, R., Zhao, L.-S., Perillat, D., Carricato, G., Recknor, M., Du, K., Ho, H., Ellis, T., Gamez, J., … Tan, H., (2009). Label-free detection of biomolecular interactions using biolayer interferometry for kinetic characterization. Combinatorial Chemistry & High Throughput Screening, 12, 791-800.
Krone, J. R., Nelson, R. W., Dogruel, D., Williams, P., & Granzow, R. (1997). BIA/MS: Interfacing biomolecular interaction analysis with mass spectrometry. Analytical Biochemistry, 244, 124-132.
Sönksen, C. P., Nordhoff, E., Jansson, Ö., Malmqvist, M., & Roepstorff, P. (1998). Combining MALDI mass spectrometry and biomolecular interaction analysis using a biomolecular interaction analysis instrument. Analytical Chemistry, 70, 2731-2736.
Natsume, T., Nakayama, H., Jansson, Ö., Isobe, T., Takio, K., & Mikoshiba, K. (2000). Combination of biomolecular interaction analysis and mass spectrometric amino acid sequencing. Analytical Chemistry, 72, 4193-4198.
Lopez, F., Pichereaux, C., Burlet-Schiltz, O., Pradayrol, L., Monsarrat, B., & Estève, J.-P. (2003). Improved sensitivity of biomolecular interaction analysis mass spectrometry for the identification of interacting molecules. Proteomics, 3, 402-412.
Remy-Martin, F., El Osta, M., Lucchi, G., Zeggari, R., Leblois, T., Bellon, S., Ducoroy, P., & Boireau, W. (2012). Surface plasmon resonance imaging in arrays coupled with mass spectrometry (SUPRA-MS): Proof of concept of on-chip characterization of a potential breast cancer marker in human plasma. Analytical and Bioanalytical Chemistry, 404, 423-432.
Nedelkov, D., Tubbs, K. A., & Nelson, R. W. (2006). Surface plasmon resonance-enabled mass spectrometry arrays. Electrophoresis, 27, 3671-3675.
Nedelkov, D. (2007). Development of surface plasmon resonance mass spectrometry array platform. Analytical Chemistry, 79, 5987-5990.
Bellon, S., Buchmann, W., Gonnet, F., Jarroux, N., Anger-Leroy, M., Guillonneau, F., & Daniel, R. (2009). Hyphenation of surface plasmon resonance imaging to matrix-assisted laser desorption ionization mass spectrometry by on-chip mass spectrometry and tandem mass spectrometry analysis. Analytical Chemistry, 81, 7695-7702.
Kim, M., Park, K., Jeong, E.-J., Shin, Y.-B., & Chung, B. H. (2006). Surface plasmon resonance imaging analysis of protein-protein interactions using on-chip-expressed capture protein. Analytical Biochemistry, 351, 298-304.
Geitmann, M., & Danielson, U. H (2004). Studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology. Analytical Biochemistry, 332, 203-214.
Bouffartigues, E., Leh, H., Anger-Leroy, M., Rimsky, S., & Buckle, M. (2007). Rapid coupling of surface plasmon resonance (SPR and SPRi) and ProteinChipTM based mass spectrometry for the identification of proteins in nucleoprotein interactions. Nucleic Acids Research, 35, e39-e39.
Gamsjaeger, R., Kariawasam, R., Bang, L. H., Touma, C., Nguyen, C. D., Matthews, J. M., Cubeddu, L., & Mackay, J. P. (2013). Semiquantitative and quantitative analysis of protein-DNA interactions using steady-state measurements in surface plasmon resonance competition experiments. Analytical Biochemistry, 440, 178-185.
Beseničar, M., Maček, P., Lakey, J. H., Anderluh, G. (2006). Surface plasmon resonance in protein-membrane interactions. Chemistry and Physics of Lipids, 141, 169-178.
Safina, G. (2012). Application of surface plasmon resonance for the detection of carbohydrates, glycoconjugates, and measurement of the carbohydrate-specific interactions: A comparison with conventional analytical techniques. A critical review. Analytica Chimica Acta, 712, 9-29.
Przybylski, C., Gonnet, F., Saesen, E., Lortat-Jacob, H., & Daniel, R. (2020) Surface plasmon resonance imaging coupled to on-chip mass spectrometry: A new tool to probe protein-GAG interactions. Analytical and Bioanalytical Chemistry, 412, 507-519.
Machen, A. J., O'neil, P. T., Pentelute, B. L., Villar, M. T., Artigues, A., & Fisher, M. T. (2018). Analyzing dynamic protein complexes assembled on and released from biolayer interferometry biosensor using mass spectrometry and electron microscopy. Journal of Visualized Experiments, 57902.
Andrzejewska, Z., Nevo, N., Thomas, L., Chhuon, C., Bailleux, A., Chauvet, V., Courtoy, P. J., Chol, M., Guerrera, I. C., & Antignac, C. (2016). Cystinosin is a component of the vacuolar H+-ATPase-ragulator-rag complex controlling mammalian target of rapamycin complex 1 signaling. Journal of the American Society of Nephrology, 27, 1678-1688.
Lipecka, J., Chhuon, C., Bourderioux, M., Bessard, M.-A., Van Endert, P., Edelman, A., & Guerrera, I. C. (2016). Sensitivity of mass spectrometry analysis depends on the shape of the filtration unit used for filter aided sample preparation (FASP). Proteomics, 16, 1852-1857.
Chhuon, C., Zhang, S.-Y., Jung, V., Lewandowski, D., Lipecka, J., Pawlak, A., Sahali, D., Ollero, M., & Guerrera, I. C. (2020). A sensitive S-Trap-based approach to the analysis of T cell lipid raft proteome. Journal of Lipid Research, 61, 1512-1523.
Cox, J., & Mann, M. (2008). MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nature Biotechnology, 26(6), 1367-1372.
Tyanova, S., Temu, T., Sinitcyn, P., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016). The Perseus computational platform for comprehensive analysis of (prote)omics data. Nature Methods, 13, 731-740.