A new method to constrain droplets during evaporation to fabricate MALDI (Matrix Assisted Laser Desorption Ionization) targets is described. Superhydrophobic silicon nanowire (NW) surfaces with laser ablated hydrophilic (LAH) spots are used to improve the sensitivity of MALDI time-of-flight mass spectrometry (MALDI-TOF MS). MALDI is currently one of the most widely used tools for identification of biomolecules. The advantages of MALDI include low detection limits, soft ionization and analyses of both complex mixtures and large biomolecules, such as whole proteins. However, the UV laser spot size used to ionize and desorb the protein/matrix samples is typically only ~100µm in diameter, while the standard MALDI target spot is 2.5 mm in diameter. Thus, only a small fraction (less than 1/25, not accounting for depth of ablation) of the sample is desorbed/ionized with each shot of the laser. This work utilizes fractal NW surfaces with LAH spots to concentrate the protein/matrix samples down to a ~250 µm diameter spot size, improving both efficiency of laser desorption/ionization and sensitivity of the instrument. Myoglobin samples at various concentrations were analyzed by MALDI on a standard MALDI plate and on NW supports with LAH spots. Accumulations of signals were recorded and averaged to represent both the efficiency of obtaining a signal and the sensitivity of the instrument. Preliminary results indicate an average improvement in MALDI sensitivity for whole proteins by a factor of 5. Previous methods utilize hydrophobic, Teflon-coated plates with gold, hydrophilic “anchor” spots. However, the drops migrate away from the anchor spots during evaporation. The surfaces in this work completely confine and concentrate the samples during evaporation. This phenomenon offers an advantage over previous methods because the NW supports may be used for feasible automation of MALDI and coupling with separations techniques, such as capillary electrophoresis.