Scientists made a special coating that sticks a tiny peptide called GHK onto a gold surface, then adds copper ions so that a big protein (human serum albumin) lines up in a specific way. They used fancy sensors to watch how the protein attached and built a math model to predict coverage. The work is about engineering surfaces, not about taking GHK as a supplement.

Protein immobilization in a specific conformation or orientation at an interface is influenced by specific interactions with the outer layer of the surface. A strategy to build-up a complex construct which is able to orient protein molecules, based on metal-cation chelation processes, is reported. The proposed methodology implies the formation of a mercaptoundecanoic acid monolayer on a gold surface that is activated to attach covalently the tripeptide glycyl-l-histidyl-l-lysine (GHK) on the surface, whose sites are then employed to chelate copper ions, providing a selective platform for the orientation of human serum albumin (HSA) molecules. The protein adsorption process on GHK and GHK-Cu(II)-complex surfaces was monitored by the in situ quartz crystal microbalance with dissipation monitoring (QCM-D) and force spectroscopy technique. The changes in frequency and dissipation factor as well as the D- f plots from QCM-D measurements help to characterize the changes in the protein conformation and are confirmed by force curve spectroscopy results. An improved kinetic model, based on random sequential adsorption with variable protein footprints, has been developed to predict and simulate the experimentally found HSA average surface coverage onto the GHK and GHK-Cu(II)-complex surfaces.