Supplementary Material for: Isoform-specific oxidative modifications of tropoelastin by HOCl and MPO alter protein self-assembly

This upload contains supplementary material supporting the manuscript titled "Isoform-specific oxidative modifications of tropoelastin by HOCl and MPO alter protein self-assembly."It includes extended methods, supplementary figures (S1–S2), and tables (S1–S8) detailing mass spectrometry results, peptide oxidation sites, and coacervation data. These materials are intended for use alongside the journal article submitted to Redox Report in August 2025. The files contain Supplementary Methods. Figure S1: MS/MS Spectra of multiply modified peptide LPGGYGLPYTTGK Figure S2: Annotated MS/MS Spectra of Oxidatively Modified Peptides in Tropoelastin Isoforms TE2 and TE6. Table S1: Theoretical trypsin-digested peptides from tropoelastin isoforms 2 and 6(Includes peptide IDs, sequences, residue positions, and isoform-specific annotations) Table S2: Modification sites and their corresponding peptides identified in TE2 and TE6(Lists site-specific chlorination and oxidation modifications detected via LC-MS/MS) Table S3: Frequency of amino acid residues susceptible to HOCl modification in TE2 and TE6(Summarizes the detection rates and modification status of tyrosine and cysteine residues) Table S4: Retention times for peptide LPGGYGLPYTTGK with different chlorination modifications in TE2 and TE6 (Includes RT values for mono- and di-chlorinated proteoforms under HOCl and MPO treatment) Table S5: Quantitative MS data for TE2 under HOCl treatment Table S6: Quantitative MS data for TE2 under MPO treatment Table S7: Quantitative MS data for TE6 under HOCl treatment Table S8: Quantitative MS data for TE6 under MPO treatment(Tables S5–S8 include label-free quantification of peptide intensities and modification types)