Human serum albumin–copper complex

Human serum albumin (HSA) is the most abundant plasma protein and serves as a key transporter of metal ions, notably copper (Cu(II)), in blood. Roughly 15% of circulating plasma copper is bound to albumin, with the remainder mainly associated with ceruloplasmin (70%) and alpha-2-macroglobulin (10%). Albumin binds Cu(II) with high affinity at its amino-terminal site, forming a labile pool readily exchangeable with cellular transporters such as copper transporter 1 (Ctr1). This copper pool is essential for distribution and homeostasis, but HSA–copper is not itself a conventional pharmacological target[2][3][6][1]. Albumin–copper interactions play important roles in detoxifying redox-active copper and delivering copper to tissues, and are relevant for understanding oral copper uptake, inherited copper metabolism disorders, and the pharmacodynamics of certain copper-chelating anticancer drugs[1][2][4][6].

Other names

Albumin–copper complexHSA–copper complexHuman serum albumin–Cu(II) complex

Chelation and removal of Cu(II) from albumin binding site