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https:\/\/doi.org\/10.1016\/j.jsb.2020.107604<\/p>\n
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Globular domains flanking amyloid-forming regions can prevent the formation of cross-\u03b2 amyloids.<\/p>\n<\/dd>\n
Coarse-grained and rigid body simulation show that these proteins form cross-\u03b2 oligomers.<\/p>\n<\/dd>\n
The oligomerisation may provide insight into phase separation of proteins with amyloidogenic regions.<\/p>\n<\/dd>\n
This study opens up opportunities for design of nano-oligomers with functional domains.<\/p>\n<\/dd>\n<\/dl>\n<\/div>\n<\/div>\n
Insoluble amyloid fibrils formed by self-assembly of amyloidogenic regions of proteins have a cross-\u03b2-structure. In this work, by using targeted molecular dynamics and rigid body simulation, we demonstrate that if a protein consists of an amyloidogenic region and a globular domain(s) and if the linker between them is short enough, such molecules cannot assemble into amyloid fibrils, instead, they form oligomers with a defined and limited number of \u03b2-strands in the cross-\u03b2 core. We show that this blockage of the amyloid growth is due to the steric repulsion of the globular structures linked to amyloidogenic regions. Furthermore, we establish a relationship between the linker length and the number of monomers in such nanoparticles. We hypothesise that such oligomerisation can be a yet unrecognised way to form natural protein complexes involved in biological processes. Our results can also be used in protein engineering for designing soluble nanoparticles carrying different functional domains.<\/p>\n
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https:\/\/doi.org\/10.1016\/j.jsb.2020.107604 Highlights \u2022 Globular domains flanking amyloid-forming regions can prevent the formation of cross-\u03b2 amyloids. \u2022 Coarse-grained and rigid body simulation show that these proteins form cross-\u03b2 oligomers. \u2022 The oligomerisation may provide insight into phase separation of proteins with amyloidogenic regions. \u2022 This study opens up opportunities for design of nano-oligomers with functional […]<\/p>\n","protected":false},"author":65,"featured_media":3490,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[1],"tags":[],"_links":{"self":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3488"}],"collection":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/users\/65"}],"replies":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/comments?post=3488"}],"version-history":[{"count":1,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3488\/revisions"}],"predecessor-version":[{"id":3491,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3488\/revisions\/3491"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media\/3490"}],"wp:attachment":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media?parent=3488"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/categories?post=3488"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/tags?post=3488"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}