a-lactalbumin (LA) in its molten globule (MG) state at low pH forms amyloid fibrils. Here, we have studied the aggregation propensities of LA derivatives characterized by a single peptide bond fission (1–40⁄41–123, named Th1-LA) or a deletion of a chain segment of 12 amino acid resi-dues located at the level of the b-subdomain of the native protein (1– 40⁄53–123, named desb-LA). We have also compared the early stages of the aggregation process of these LA derivatives with those of intact LA
