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Peptide pull-down (PPD) is an in vitro affinity purification technique used to detect and identify proteins that interact with specific peptide sequences. In this method, biotinylated synthetic peptides serve as “baits” immobilized on streptavidin-coated magnetic or agarose beads. After incubation with cell lysates or nuclear extracts, non-specifically bound proteins are removed through washing steps, and specific interacting proteins are eluted and enriched for subsequent analysis by SDS-PAGE, Western Blot, or mass spectrometry (LC-MS/MS). PPD is particularly suited for studying protein-protein interactions mediated by short linear motifs (SLiMs) and for investigating the regulatory effects of post-translational modifications (e.g., histone modifications) on protein interactions. When combined with quantitative proteomic approaches such as SILAC (Stable Isotope Labeling by Amino Acids in Cell Culture), PPD can effectively discriminate specific interactors from background noise, enabling high-sensitivity interactome screening.