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Milner, Alshammari, and Platts (2021), in Inorganica Chimica Acta , used molecular modeling to characterize DAHK's copper-binding geometry, binding-energy landscape, and electronic structure, finding that the peptide can adopt multiple stable Cu coordination configurations depending on solvent and pH with the aspartyl carboxylate and histidyl imidazole groups both contributing to a flexible, multi-dentate binding environment.[2] This structural flexibility is of interest for understanding copper transport and redox cycling in albumin-mediated copper homeostasis, and for research into copper dysregulation in oxidative stress and neurodegenerative disease contexts though it's worth flagging that this line of evidence is computational/structural rather than cell- or animal-based functional data

Researchers continue to explore BPC-157 in controlled laboratory environments to better understand peptide behavior and biochemical mechanisms