Extracellular signal-regulated kinase 2 (ERK2) is a mitogen-activated protein kinase and serves as an important relay in phosphorylation signaling cascades.  A substrate (Sub-D) was predicted through computational modeling studies to bind at the D-recruitment site (DRS) on ERK2. Using solid-phase peptide synthesis, Sub-D was synthesized along with anionic and cationic derivatives to compare differences in kinase activity when introduced to ERK2 in the presence or absence of oxidative challenge. Additionally, the predicted interactions between ERK2 and derivatives will be characterized by X-ray crystallography in order to develop a deeper understanding how oxidative stress affects the phosphorylation efficiency of ERK2.

Synthesis of computationally derived ERK2 substrates to probe kinase activity during oxidative stress

2019 Spring National Meeting

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