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The extracted teeth were carefully washed and disinfected. The enamel and cementum were removed with a diamond bur. The teeth were stored in phosphate-buffered saline at 4 °C. After removal of pulpal tissue to avoid protein impurities, the remaining dentine was subsequently cryogenically ground using a TissueLyser II (QIAGEN, Germany), and the resulting dentin powder was maintained in liquid nitrogen to preserve its structural integrity. To evaluate the effect of prefractionation on dentin proteome coverage, protein extracts obtained  from EDTA-demineralized dentin were processed using three parallel strategies: no fractionation,  protein-level fractionation, and peptide-level fractionation (Figure 2). In the unfractionated  workflow, samples underwent SP4 digestion followed by liquid chromatography-tandem mass  spectrometry (LC-MS/MS analysis). For protein-level fractionation, proteins were separatedby SDS-PAGE, in-gel digested, and analyzed by LC-MS/MS. For peptide-level fractionation, SP4  digested peptides were further separated using either strong cation exchange (SCX) or high-pH reversed-phase (HpH) chromatography before LC-MS/MS analysis."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Samples were converted to the open mzML format using MSConvert (20) and then processed with DIA-NN (21) version 1.8.1. The spectral library was the DIA-NN in-silico predicted spectral library, built using the UniProt reference human proteome (UP00005640, accessed August 182023) (22), which includes isoforms (82,022 protein entries, 20,510 genes). The spectral library was generated with default settings, allowing for 1 missed cleavage and no variable modifications.Samples were processed with mass accuracy set to 10 ppm, heuristic protein inference turned off, match between runs enabled, and the neural network classifier set to double-pass mode. Precursors were filtered to 1% FDR. For protein inference, the DIA-NN peptide output was summarised to the gene group level using the ‘diann’ R package implementation of the MaxLFQ algorithm (21, 23) using a 1 % FDR cutoff at both the precursor and gene group level. Protein groups were filtered to include only those with no missing values in at least two groups, and subsequently, missing values were imputed using half the minimum observed value for each protein group. Significance was determined by way of ANOVA using the ‘aov’ function from the default R ‘stats’ package (R Core Team, 2022) and defined as those protein groups with p < 0.05 after multiple testing correction using the Benjamini-Hochberg method (24)."],"omics_type":["Proteomics"],"labhead":["Mohamed Jamal"],"instrument_platform":[""],"labhead_affiliation":["Hamdan Bin Mohammed College of Dental Medicine, Mohammed Bin Rashid University of Medicine and Health Sciences, Dubai Health, Dubai, UAE"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["bushra.gull@dubaihealth.ae"],"publication":["41839003 Khalil M, Gull B, Alhimairi S, Giddey AD, Jamal M. Proteomic Analysis of Human Dentine Matrix Extracts by Peptide-Level High-pH Reversed-Phase Fractionation. J Proteome Res. 2026 10.1021/acs.jproteome.5c01067"],"submitter_affiliation":["Mohammed Bin Rashid University of Medicine and Health Sciences"],"submitter_country":["United Arab Emirates"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analysis of human dentin matrix extracts by  peptide-level high-pH reverse-phase fractionation","description":"Proteomics research has increasingly focused on human cells, tissues, and fluids;  however, comprehensive data regarding dental tissues remain limited. Dentin, a mineralized  component of the tooth, contains structural proteins and bioactive molecules that, upon release,  can modulate pulp cell activity and facilitate regeneration. Therefore, an understanding of the  protein composition of dentin is of considerable importance.  Previous studies have reported a limited number of proteins, and technical difficulties have often  hindered replication. Furthermore, traditional extraction methods rely on strong acids, which are  not clinically relevant. In this technical note, we introduce a workflow that combines EDTA-based  dentin extraction under clinically relevant conditions with peptide-level fractionation using high-pH reverse-phase chromatography. This approach was compared against unfractionated samples  (control), protein-level fractionation via SDS-PAGE, and peptide-level fractionation utilizing  strong cation exchange (SCX), all followed by LC-MS/MS analysis.  This workflow facilitated the identification of 514 proteins, compared with 238 (unfractionated  control), 428 (SDS-PAGE), and 193 (SCX). High-pH reverse-phase chromatography contributed  217 unique identifications, surpassing the number of unique fractions identified through the other  techniques. Although this methodology has been utilized in other protein systems, it has not  previously been applied to dentin matrix extracts and represents a promising approach for  enhancing the comprehensiveness of protein 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