Neuroendocrine cells secrete neuropeptides in efforts to maintain dynamic equilibrium in response to stress. Neuropeptides are short chains of amino acids that are low in abundance and are transient in nature. However, in spite of notable successes in characterizing neuropeptide structure and function, localization of neuropeptides by mass spectrometry imaging have been limited by inherent low spatial resolution of this technique compared to the resolution offered by immunohistochemistry techniques. We hypothesize that neuropeptides will be unmodified by reactants that would otherwise catabolize or delocalize altogether larger proteases and other ion suppressors. We use this to develop methods for enhancing sensitivity of mass spectrometry imaging for detection of neuropeptides. This system allows us to characterize the changes in neuropeptide expression due to a variety of stressors in a crustacean model organism. My role in this process has been designing the mass spectrometry imaging experiments, optimizing the sample preparation parameters, and collecting neuroendocrine tissues from crustaceans exposed to hypoxia stress for mass spectrometry analysis.