Profiling polyamine-protein interactions in live cells through photoaffinity labeling.

ABSTRACT: Polyamines are essential metabolites that play a crucial role in regulating key cellular processes. While previous studies have shown that polyamines modulate protein function through non-covalent interactions, the lack of robust analytical methods has limited the systematic identification of these interactions in living cells. To address this challenge, we synthesized a series of novel photoaffinity probes and applied them to a model cell line, identifying over 400 putative protein interactors with remarkable polyamine analog structure-dependent specificity. Analysis of probe-modified peptides revealed photocrosslinking sites for dozens of protein binders and demonstrated that all but one of the probes, the spermine analog, were intracellularly stable. The interaction profiles of these pr

SUBMITTER: Zakrzewski M 

PROVIDER: S-EPMC12461607 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature