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In this study, the effects of homocysteine thiolactone (HCTL) and hydrogen peroxide (H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub>) on the conformation and fibrillation propensity of the A\u03b2<jats:sub>25\u201335<\/jats:sub> peptide were investigated. Both HCTL and H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> induced amino acid modifications along with alteration in aggregation propensity. Methionine (Met)\u201035 was oxidized by H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> and aggregation was attenuated following the increased hydrophilicity of the peptide due to sulfoxide\/sulfone formation. The HCTL\u2010modified lysine (Lys\u201028) residue destabilizes the structure of the peptide, which leads to fibrillation. Our studies provide important information regarding the relationship between amino acid modifications and the amyloid fibrillation process.<\/jats:p>","DOI":"10.1002\/1873-3468.14583","type":"journal-article","created":{"date-parts":[[2023,1,25]],"date-time":"2023-01-25T04:35:11Z","timestamp":1674621311000},"page":"1041-1051","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Homocysteine thiolactone and <scp>H<sub>2<\/sub>O<sub>2<\/sub><\/scp> induce amino acid modifications and alter the fibrillation propensity of the A\u03b2<sub>25\u201335<\/sub> peptide"],"prefix":"10.1002","volume":"597","author":[{"given":"Sudipta","family":"Bag","sequence":"first","affiliation":[{"name":"Department of Chemistry Indian Institute of Technology Kharagpur  India"},{"name":"Sister Nivedita University  New Town 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