Agents mobilizing Cu(II) from the inert ATCUN complex need both high affinity and a specific chelating structure.

This biochemistry study examines how small molecules can facilitate copper ion transfer from tightly-bound ATCUN peptide complexes to other receptors, mimicking physiological copper handling. The researchers found that histidine and His-Leu dipeptides specifically accelerate copper mobilization through a two-coordinate binding mechanism. The findings provide mechanistic insight into how peptide-based copper delivery systems could improve bioavailability and cellular copper transport—directly relevant to copper-peptide supplements like GHK-Cu that depend on efficient copper bioavailability.

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Copper transfer from ATCUN complexes requires both high affinity and specific chelate geometry, informing how GHK-Cu may deliver copper bioavailably.

Read more on J Inorg Biochem →

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