Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes

Lucas S Dantas; Alex Inague; Adriano Britto Chaves-Filho; Sayuri Miyamoto

doi:10.1016/j.dib.2020.105850

Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes

Data Brief. 2020 Jun 12:31:105850. doi: 10.1016/j.dib.2020.105850. eCollection 2020 Aug.

Authors

Lucas S Dantas¹, Alex Inague¹, Adriano Britto Chaves-Filho¹, Sayuri Miyamoto¹

Affiliation

¹ Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil.

Abstract

Metal-deficient Cu,Zn-superoxide dismutase (apo-SOD1) is associated with the formation of SOD1 aggregates that accumulate in ALS disease. The data supplied in this article support the accompanying publication showing SOD1 modification and aggregation induced by lipid aldehydes [1]. Here, we present the LC-MS/MS dataset on apo-SOD1 modification induced by seven different lipid aldehydes: 4-hydroxy-2-hexenal (HHE), 4-hydroxy-2-nonenal (HNE), 2-hexen-1-al (HEX), 2,4-nonadienal (NON), 2,4-decadienal (DEC) or secosterol aldehydes (SECO-A or SECO-B). Modified protein samples were digested with trypsin and sequenced by a LC coupled to a Q-TOF instrument. Protein sequencing and peptide modification analysis was performed by Mascot 2.6 (Matrix Science) and further validated by manual inspection. Mass spectrometry data (RAW files) obtained in this study have been deposited to MassIVE and the observed peptide-aldehyde adducts can be used in further studies exploring SOD1 modifications in vivo.

Keywords: Lipid aldehydes; Lipid electrophiles; Oxysterol; PTM; SOD1; Secoaldehydes.