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Laboratory investigations demonstrate that GHK-Cu exhibits a copper binding affinity (log K = 16.1) that positions it perfectly within the physiological copper transport hierarchystronger than albumin but weaker than ceruloplasminenabling controlled copper transfer to cellular targets

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After transport across the outer membrane, iron recovered from human transferrin or lactoferrin is bound by the periplasmic protein FbpA and directed to the inner membrane transporter FbpBC (Stojiljkovic and Srinivasan, 1997), although TonB-independent iron transport processes were reported in N

Zinc and copper interact during absorption and biochemical regulation

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