DOI: 10.5281/zenodo.18279417
title: Proteomic analysis results of platelet-rich fibrin extract

description: Dataset title

Proteomic analysis of platelet-rich fibrin extract activated by cyclic low-frequency ultrasound

Dataset overview

This dataset presents a comprehensive proteomic characterization of platelet-rich fibrin extract (PRFe) obtained through cyclic low-frequency ultrasound (CLFU)–mediated activation of platelet-rich fibrin (PRF). PRF was prepared from peripheral venous blood collected from healthy adult donors and subjected to a biomimetic mechanical activation protocol to regulate platelet degranulation and protein release. The resulting PRFe was processed and analyzed to define its protein composition using mass spectrometry–based proteomics.

Sample preparation

PRF clots were generated from freshly collected human peripheral blood without anticoagulants. For PRFe preparation, PRF samples were immersed in saline and activated using a CLFU protocol involving intermittent low-frequency ultrasound stimulation. Following activation, PRFe was collected, centrifuged to remove residual fibrin components, and filtered to obtain clarified protein extracts suitable for proteomic analysis.

Proteomic analysis

Protein composition of PRFe was analyzed using liquid chromatography–tandem mass spectrometry (LC–MS/MS). Samples underwent standard proteomics workflows, including protein digestion and peptide purification prior to MS analysis. Data acquisition was performed on a high-resolution LC–MS/MS platform. Protein identification and quantification were conducted using established bioinformatics pipelines, with relative protein abundance estimated using intensity-based absolute quantification (iBAQ).

Data content

The dataset includes raw mass spectrometry files and processed protein identification and quantification results. More than 300 proteins were identified in PRFe samples. The detected proteins predominantly consist of plasma- and platelet-associated components, including albumin, transferrin, apolipoproteins, immunoglobulin chains, and other blood-derived proteins, reflecting the autologous origin of PRFe.

Functional annotation

Functional annotation and enrichment analyses were performed using Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) databases. Identified proteins were associated with biological processes related to complement activation, immune regulation, angiogenesis, extracellular matrix organization, and wound-related responses. Cellular component analysis indicated enrichment in blood microparticles, platelet α-granules, and extracellular matrix–associated compartments. KEGG pathway analysis highlighted complement and coagulation cascades and extracellular matrix–receptor interaction pathways.

Data availability and reuse

This dataset provides a qualitative overview of the protein composition of PRFe generated under a standardized, mechanically programmed activation protocol. The data may be reused for comparative studies of platelet-derived biomaterials, investigations into extracellular matrix–associated signaling, and proteomics-based analyses related to tissue regeneration, angiogenesis, and regenerative medicine.