PIRL DIVE-extraction of proteins
Ultrafast extraction of proteins from tissues using desorption by impulsive vibrational excitation.
The extraction of proteins from tissue samples represents a critical and time-consuming step in every proteomic and protein analytical approach. In general, protein extraction includes a number of different experimental steps like homogenization, lyzation and protein isolation varying in dependence of tissue type and proteins of interest. Recently, Kwiatkowski et al.  show that PIRL and the quantum mechanical effects leading to the coupling of the OH vibration to O-O translation motions, the DIVE process facilitates a rapid and gentle procedure for intact protein extraction. This transduction of absorbed photon energy into translational motions, the very degree of freedom required for ablation, is a factor of nearly 100 faster than any other material, grace of the hydrogen bond network of water (see Cowan et al., Nature 2005 , Kraemer et al. PNAS 2008 ).
Compared to classical protein extraction procedures, that lasted several days, DIVE extracts proteins from tissue samples within a few minutes in a high quantity and quality, retaining their chemical composition and enzymatic activities. Furthermore DIVE protein extracts showed to be compatible with most protein analytical techniques like immunoblotting, gel electrophoresis and mass spectrometry, minimizing time and sample loss.
- Kwiatkowski, M., et al., Ultrafast extraction of proteins from tissues using desorption by impulsive vibrational excitation. Angew Chem Int Ed Engl, 2015. 54(1). PubMed
- Cowan, M.L., et al., Ultrafast memory loss and energy redistribution in the hydrogen bond network of liquid H2O. Nature, 2005. 434(7030). PubMed
- Kraemer, D., et al., Temperature dependence of the two-dimensional infrared spectrum of liquid H2O. Proc Natl Acad Sci U S A, 2008. 105(2). PubMed