The order of the N-terminus of Human serum albumin (HSA), more especially Asp1-Ala2-His3-Lys4, is extremely vulnerable to oxidative stress-induced metabolic alterations and degradation. This vulnerability leads to reduced affinity of the N-terminal sequence (NTS) to transition metals, particularly cobalt. This altered variant of albumin is referred to as ischemia-modified albumin (IMA).