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Currently, there are still several aspects of amyloid aggregation that are not fully understood, which negatively contributes to the development of disease\u2010altering drugs and treatments. One factor which requires a more in\u2010depth analysis is the effect of the environment on both the initial state of amyloidogenic proteins and their aggregation process and resulting fibril characteristics. In this work, we examine how lysozyme's folding state influences its amyloid formation kinetics and resulting aggregate structural characteristics under several different pH conditions, ranging from acidic to neutral. We demonstrate that both the initial state of the protein and the solution's pH value have a significant combined effect on the variability of the resulting aggregate secondary structures, as well as their stabilities, interactions with amyloid\u2010specific dye molecules, and self\u2010replication properties.<\/jats:p>","DOI":"10.1002\/pro.4888","type":"journal-article","created":{"date-parts":[[2023,12,28]],"date-time":"2023-12-28T06:53:30Z","timestamp":1703746410000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different <scp>pH<\/scp> conditions"],"prefix":"10.1002","volume":"33","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8368-6188","authenticated-orcid":false,"given":"Mantas","family":"Ziaunys","sequence":"first","affiliation":[{"name":"Institute of Biotechnology, Life Sciences 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