phosphopeptide

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.

Casein phosphopeptide is a biochemical reagent that can be used as a biomaterial for life science related research and as a sulfonylation reagent for organic synthesis and drug discovery.

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

CGP78850 is a potent and selective Grb2 SH2-phosphopeptide interaction antagonist with potential applications in cancer research.

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).

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

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.

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

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

PKA Regulatory Subunit II Substrate (RII phosphopeptide) is a tool peptide derived from the regulatory subunit Type II (RII) of cyclic adenosine monophosphate-dependent protein kinase (PKA). It is commonly used to simulate the phosphorylation activity of protein kinases and to assess the activity of protein phosphatases by serving as a specific substrate.