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Acrolein sequestering ability of the endogenous tripeptide glycyl-histidyl-lysine (GHK): characterization of conjugation products by ESI-MSn and theoretical calculations

The membrane pellet was homogenized and solubilized by gentle nutation for 2 hours at 4 C in buffer consisting of 20 mM Tris-Cl (pH 8.0), 150 mM NaCl, 1% Dodecyl--D-Maltosid (w/v, DDM), and 20 M DNQX, followed by centrifugation at 200,000 g for 30 min to remove insoluble material

Subsequent copper binding induces aberrant oligomerization of these proteins, disrupting the TCA cycle and initiating cell death [55]

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