Dataset Information

Dear-DIA^XMBD: Deep Autoencoder Enables Deconvolution of Data-Independent Acquisition Proteomics.

ABSTRACT: Data-independent acquisition (DIA) technology for protein identification from mass spectrometry and related algorithms is developing rapidly. The spectrum-centric analysis of DIA data without the use of spectra library from data-dependent acquisition data represents a promising direction. In this paper, we proposed an untargeted analysis method, Dear-DIA^XMBD, for direct analysis of DIA data. Dear-DIA^XMBD first integrates the deep variational autoencoder and triplet loss to learn the representations of the extracted fragment ion chromatograms, then uses the k-means clustering algorithm to aggregate fragments with similar representations into the same classes, and finally establishes the inverted index tables to determine the precursors of fragment clusters between precursors and peptides and between fragments and peptides. We show that Dear-DIA^XMBD performs superiorly with the highly complicated DIA data of different species obtained by different instrument platforms. Dear-DIA^XMBD is publicly available at https://github.com/jianweishuai/Dear-DIA-XMBD.

SUBMITTER: He Q

PROVIDER: S-EPMC10292580 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature

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Publications

Dear-DIAXMBD: Deep Autoencoder Enables Deconvolution of Data-Independent Acquisition Proteomics.

He Qingzu Q Zhong Chuan-Qi CQ Li Xiang X Guo Huan H Li Yiming Y Gao Mingxuan M Yu Rongshan R Liu Xianming X Zhang Fangfei F Guo Donghui D Ye Fangfu F Guo Tiannan T Shuai Jianwei J Han Jiahuai J

Research (Washington, D.C.) 20230626

Data-independent acquisition (DIA) technology for protein identification from mass spectrometry and related algorithms is developing rapidly. The spectrum-centric analysis of DIA data without the use of spectra library from data-dependent acquisition data represents a promising direction. In this paper, we proposed an untargeted analysis method, Dear-DIAXMBD, for direct analysis of DIA data. Dear-DIAXMBD first integrates the deep variational autoencoder and triplet loss to ...[more]

PMID: 37377457

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Project description:Methodologies that facilitate high-throughput proteomic analysis are a key step toward moving proteome investigations into clinical translation. Data independent acquisition (DIA) has potential as a high-throughput analytical method due to the reduced time needed for sample analysis, as well as its highly quantitative accuracy. However, a limiting feature of DIA methods is the sensitivity of detection of low abundant proteins and depth of coverage, which other mass spectrometry approaches address by two-dimensional fractionation (2D) to reduce sample complexity during data acquisition. In this study, we developed a 2D-DIA method intended for rapid- and deeper-proteome analysis compared to conventional 1D-DIA analysis. First, we characterized 96 individual fractions obtained from the protein standard, NCI-7, using a data-dependent approach (DDA), identifying a total of 151,366 unique peptides from 11,273 protein groups. We observed that the majority of the proteins can be identified from just a few selected fractions. By performing an optimization analysis, we identified six fractions with high peptide number and uniqueness that can account for 80% of the proteins identified in the entire experiment. These selected fractions were combined into a single sample which was then subjected to DIA (referred to as 2D-DIA) quantitative analysis. Furthermore, improved DIA quantification was achieved using a hybrid spectral library, obtained by combining peptides identified from DDA data with peptides identified directly from the DIA runs with the help of DIA-Umpire. The optimized 2D-DIA method allowed for improved identification and quantification of low abundant proteins compared to conventional unfractionated DIA analysis (1D-DIA). We then applied the 2D-DIA method to profile the proteomes of two breast cancer patient-derived xenograft (PDX) models, quantifying 6,217 and 6,167 unique proteins in basal- and luminal- tumors, respectively. Overall, this study demonstrates the potential of high-throughput quantitative proteomics using a novel 2D-DIA method.

Dataset Information

Dear-DIA^XMBD: Deep Autoencoder Enables Deconvolution of Data-Independent Acquisition Proteomics.

Publications

Dear-DIA<sup>XMBD</sup>: Deep Autoencoder Enables Deconvolution of Data-Independent Acquisition Proteomics.

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