PubMed · 16570390
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Rajendrani Mukhopadhyay. 2006-03-01. Diving into droplets.. https://doi.org/10.1021/ac069373u
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We have carried out a simultaneous thermal denaturation and trypsin digestion of proteins using a temperature-controllable microreactor. This is a simple and rapid sample preparation technique for use before matrix-assisted laser desorption ionization time-of-flight mass spectrometry. In contrast to a conventional sample preparation method, which involves several chemical treatments, our sample preparation was performed using only trypsin digestion with the thermal denaturation of the target protein. Optimization of the reactor operational parameters for trypsin digestion using a temperature-controllable microreactor was carried out. The entire trypsin digestion procedure took about 11 min, and consisted of 1 min for the thermal denaturation of the sample protein (3 microl, 0.2 microM) at 85 degrees C, and 10 min for digestion of the protein at 37 degrees C. The resulting sequence coverage ranged from 24% to 57%, which was sufficient for practical protein identification.
In this Letter, the phenomena and parameters governing the nanoscale dispensing of liquid through an apertured atomic force microscope probe milled by focused ion beam lithography are characterized in detail. We show that the size of deposited droplets can be reproducibly defined by controlling the aperture size on the probe and the surface energies of both tip outer wall and substrate surface. On the basis of these findings, tips with aperture diameter as small as 35 nm enabled the deposition of regular arrays of nanodroplets with diameter down to 70 nm on an alkylamine-modified surface. The fine control of droplet volumes down to a few tens of zeptoliters (10(-21)L) provides a unique tool for creating devices and probing the fundamentals of wetting at the nanometer scale.
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