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

被引：1

作者：

Dantas, Lucas S. ^{[1
]}

Inague, Alex ^{[1
]}

Chaves-Filho, Adriano Britto ^{[1
]}

Miyamoto, Sayuri ^{[1
]}

机构：

[1] Univ Sao Paulo, Dept Bioquim, Inst Quim, Sao Paulo, SP, Brazil

来源：

DATA IN BRIEF | 2020年 / 31卷

基金：

巴西圣保罗研究基金会;

关键词：

PTM; Lipid aldehydes; Lipid electrophiles; Secoaldehydes; Oxysterol; SOD1; CHOLESTEROL;

D O I：

10.1016/j.dib.2020.105850

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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-hydroxy2-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 . (C) 2020 The Author(s). Published by Elsevier Inc.

引用

页数：10