CGP78850 is a potent and selective Grb2 SH2-phosphopeptide interaction antagonist that holds potential for cancer research.

EPQpYEEIPIYL, a phosphopeptide, is a ligand for the Src homology 2 (SH2) domain. It activates members of the Src family, such as Lck, Hck, and Fyn, through the binding interaction with SH2 domains.

Phosphopeptide ligand for the src SH2 domain (IC50 = 42 nM); displays 30-fold higher affinity than N-acetyl-O-phosphono-Tyr-Glu-Glu-Ile-Glu (Ac-pYEEIE,).

Phosphopeptide; binds to the src SH2 domain.

Histone H1-derived peptide is a phosphopeptide with peptide substrates that consist of a sequence aligned with the optimal recognition motif for cyclin-dependent kinases (CDKs).

Phosphopeptide ligand for the src SH2 domain (IC50 = 1 μM). Blocks src interactions with EGFR and FAK.

Bractoppin is a drug-like inhibitor of phosphopeptide recognition by the human BRCA1 tandem (t)BRCT domain (IC50 = 0.074 μM), which selectively inhibits substrate binding with nanomolar potency in vitro. Structure-activity exploration suggests that Bractoppin engages BRCA1 tBRCT residues recognizing pSer in the consensus motif, pSer-Pro-Thr-Phe, plus an abutting hydrophobic pocket that is distinct in structurally related BRCT domains, conferring selectivity.

Caffeic acid-pYEEIE TFA, a non-phosphopeptide inhibitor, demonstrates strong binding affinity for the GST-Lck-SH2 domain[1].

Selective phosphopeptide substrate for glycogen synthase kinase-3 (GSK-3)