Cleavable surfactant

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A cleavable surfactant is a surfactant that can be hydrolyzed under comparatively mild conditions . Cleavable surfactants are used in protein purification in preparation for mass spectrometry .

properties

PPS.
Protease max .

Residues of surfactants such as sodium lauryl sulfate (SDS) or octyl glucoside can make the analysis of mass spectrometric data difficult. The removal of the surfactants from the peptides to be examined z. B. after an in-gel digestion is often incomplete. With electrospray ionization , surfactants interfere more than with MALDI-TOF . In contrast, membrane proteins and lipids are only water-soluble in the presence of surfactants. Therefore, cleavable surfactants have been developed which hydrolyze under mildly acidic conditions while leaving the peptides untouched, e.g. B. 3- [3- (1,1-Bisalkyloxyethyl) pyridin-1-yl] propane-1-sulfonate (PPS), PPS with methanol , 3 - {[1- (Furan-2-yl) undecyloxy] carbonylamino} propane-1-sulfonate ( Protease MAX ), 3 - [(2-methyl-2-undecyl-1,3-dioxolan-4-yl) methoxy] -1-propanesulfonate ( RapiGest SF ).

Alternatives

cleavable CHCA derivative.

Fissile amphiphilic derivatives of α-cyano-4-hydroxycinnamic acid (CHCA), which have been coupled to decanol via formaldehyde , do not have to be removed, since they can also be used as a matrix in MALDI-TOF-MS. A matrix of α-cyano-4-hydroxycinnamic acid with cetyltrimethylammonium bromide can also be used in MALDI-TOF-MS. There are matrix mixtures that are less sensitive to surfactants.

Web links

Individual evidence

  1. ^ A b J. L. Norris, NA Porter, RM Caprioli: Mass spectrometry of intracellular and membrane proteins using cleavable detergents. In: Analytical chemistry. Volume 75, Number 23, December 2003, pp. 6642-6647, doi : 10.1021 / ac034802z . PMID 14640740 .
  2. ↑ JL Norris, NA Porter, RM Caprioli: Combination detergent / MALDI matrix: functional cleavable detergents for mass spectrometry. In: Analytical chemistry. Volume 77, Number 15, August 2005, pp. 5036-5040, doi : 10.1021 / ac050460g . PMID 16053319 .
  3. ↑ a b L. Signor, E. Boeri Erba: Matrix-assisted laser desorption / ionization time of flight (MALDI-TOF) mass spectrometric analysis of intact proteins larger than 100 kDa. In: Journal of visualized experiments: JoVE. Number 79, 2013, S., doi : 10.3791 / 50635 . PMID 24056304 . PMC 3857990 (free full text).
  4. ↑ X. Ye, DJ Johann, RM Hakami, Z. Xiao, Z. Meng, RG Ulrich, HJ Issaq, TD Veenstra, J. Blonder: Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS / MS. In: Journal of proteomics. Volume 73, number 1, November 2009, pp. 112-122, doi : 10.1016 / j.jprot.2009.08.008 . PMID 19709643 . PMC 3159575 (free full text).
  5. ↑ T. Nabetani, A. Makino, F. Hullin-Matsuda, TA Hirakawa, S. Takeoka, N. Okino, M. Ito, T. Kobayashi, Y. Hirabayashi: Multiplex analysis of sphingolipids using amine-reactive tags (iTRAQ) . In: Journal of lipid research. Volume 52, Number 6, June 2011, pp. 1294-1302, doi : 10.1194 / jlr.D014621 . PMID 21487068 . PMC 3090250 (free full text).
  6. ^ R. Gottardo, A. Chiarini, I. Dal Prà, C. Seri, C. Rimondo, G. Serpelloni, U. Armato, F. Tagliaro: Direct screening of herbal blends for new synthetic cannabinoids by MALDI-TOF MS. In: Journal of Mass Spectrometry Volume 47, Number 1, January 2012, pp. 141-146, doi : 10.1002 / jms.2036 . PMID 22282100 .