“…The TEM micrographs show that both UG and 2G κ-CN B are present as curly and rugged surface linear aggregates, which aligns with Chun et al (2012) who observed thicker fibrils with a rugged surface using unreduced forms of κ-CN, while Ecroyd et al (2008) , Ecroyd et al (2010) , Leonil et al (2008) , and Pan and Zhong (2015) observed substantially longer fibrils with a smooth surface using reduced forms of κ-CN. Although disulphide bond reduction does not significantly affect the secondary and tertiary structure of κ-CN ( Farrell et al, 2003 ), it is believed that the ability of κ-CN to form oligomers, and the subsequent propensity for amyloid fibril formation, is influenced by changes in the number of disulphide bonds links of cysteine 11 and cysteine 88 ( Hewa Nadugala et al, 2022 ; Rasmussen et al, 1992 ). This indicates that β-sheet assembly might be different with the presence or absence of disulphide bonds during fibril formation.…”