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Description

Zeidler, J

Caractersticas: Limpia

Zaffagnini et al., 2016

Since there are no crystal structures of the Nrf2/MafG interaction available to guide the design of the Nrf2 peptides, they utilized AlphaFold to predict the structure of the Nrf2/MafG heterodimer, then used the AlphaFold model to determine the best region to target for inhibition and designed three 16-amino-acid peptides that cover the predicted binding domain, they also used the model to determine the best locations for staples, specifically focusing on locations unlikely to interrupt the binding of the N1S to MafG