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In vitro, peptide assembly leads to amyloid-like fibres that have high stability, resistance to degradation and high tensile strength. Remarkably, despite the lack of any obvious sequence similarity between these fibrillogenic proteins and peptides, all amyloid fibrils share common structural characteristics and their underlying structure is known as \u2018cross-\u03b2\u2019. Nature is rich in \u03b2-sheet protein assemblies such as spider silk and other \u2018useful\u2019 amyloids such as curli from Escherichia coli, where the strength of fibrils is fundamental to their function.<\/jats:p>","DOI":"10.1042\/bst0370671","type":"journal-article","created":{"date-parts":[[2009,7,23]],"date-time":"2009-07-23T14:51:25Z","timestamp":1248360685000},"page":"671-676","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Structural integrity of \u03b2-sheet assembly"],"prefix":"10.1042","volume":"37","author":[{"given":"Karen\u00a0E.","family":"Marshall","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex, Falmer BN1 9QG, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louise\u00a0C.","family":"Serpell","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex, Falmer BN1 9QG, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2009,7,22]]},"reference":[{"key":"2021111719172075300_B1","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1098\/rstb.2000.0758","article-title":"The structural basis of protein folding and its links with human disease","volume":"356","author":"Dobson","year":"2001","journal-title":"Philos. 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