Overview
Post-translational modifications, often abbreviated as PTMs, influence protein behavior, localization, and interaction patterns in many biological systems. Because full-length proteins can be complex and difficult to work with in isolation, researchers frequently use peptides as simplified models to investigate PTM behavior. Peptides offer direct control over modification sites, surrounding sequence context, and overall composition, making them valuable tools for PTM mapping and analysis.
Synthetic peptides can be prepared with defined phosphorylation, acetylation, methylation, or other modification mimetics at specific residues. These constructs are then used in biochemical assays, analytical workflows, and calibration sets to study how PTMs affect recognition, binding, or structural preferences. Peptides also serve as standards in mass spectrometry-based PTM analyses, where they help align retention times, fragmentation patterns, and detection thresholds.
Research Areas
- Phosphorylation-site peptides – Peptides containing defined phospho-residues support studies of recognition motifs and analytical detection strategies.
- Acetylation and methylation mimetics – Modified or mimetic residues help model regulatory patterns and structural effects associated with these PTMs.
- Synthetic PTM standards – Standardized peptides with specific modifications provide reference points for quantitative and qualitative PTM analysis.
- PTM-mapping in biochemical assays – Peptide-based systems are used to test how PTMs influence binding events, structural organization, or detection methods in controlled environments.
Through these approaches, peptide tools enable researchers to decode complex regulation patterns associated with post-translational modifications while working within streamlined and well-defined model systems.