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A similar phenomenon occurs in Parkinson's disease with the build\u2010up of Lewy bodies. The analysis of senile plaques, and other brain samples, from Alzheimer's disease and Parkinson's disease patients by matrix\u2010assisted laser desorption\/ionization mass spectrometry has advantages but also presents obstacles because of the nature of the processes utilized in isolation procedures and storage. Salts, buffers, and detergents necessary in the isolation of biological species may cause adducts and ion suppression that convolute the spectra obtained. We previously determined that amyloid\u2010beta from isolated senile plaque deposits fragment similarly to the synthetic 40 and 42 amino acid peptide when analyzed by matrix\u2010assisted laser desorption\/ionization mass spectrometry. In addition, \u03b1\u2010synuclein also fragments predictably by in\u2010source decay. This provides information that may be applied to the identification and localization of amyloid\u2010beta and \u03b1\u2010synuclein in senile plaques and intact tissue sections. Ion suppression must still be accounted for when analyzing biological samples, which makes identifying fragments at lower abundance difficult. The addition of certain transition\u2010metal salts (Cu(II), Zn(II)) to the sample prior to analysis serves to \u201cclean\u201d the spectra and allow the peptide fragments produced to be observed with a much higher signal to noise and occasionally, improved resolution. We present a systematic study of incubation with different metal salts and their impact on the quality of the spectra, as well as the role of the binding of the metals to the model biological compounds, obtained for synthetic amyloid\u2010beta, synthetic \u03b1\u2010synuclein, and isolated senile plaques. The optimized sample preparation methods presented will provide for simpler and more thorough identification of these biologically relevant species in human\u2010derived samples.<\/jats:p>","DOI":"10.1002\/jms.4044","type":"journal-article","created":{"date-parts":[[2017,11,7]],"date-time":"2017-11-07T08:16:42Z","timestamp":1510042602000},"page":"162-171","source":"Crossref","is-referenced-by-count":4,"title":["Incubation with Cu(II) and Zn(II) salts enhances MALDI\u2010TOF mass spectra of amyloid\u2010beta and \u03b1\u2010synuclein toward in vivo analysis"],"prefix":"10.1002","volume":"53","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7227-5017","authenticated-orcid":false,"given":"Andrea R.","family":"Kelley","sequence":"first","affiliation":[{"name":"Department of Chemistry University of Texas at San Antonio  One UTSA Blvd. San Antonio TX USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Madeline 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