{"id":24,"date":"2001-11-16T00:00:00","date_gmt":"2001-11-16T04:00:00","guid":{"rendered":"https:\/\/www.bumc.bu.edu\/msr\/research-topics\/amyloid-model-peptides\/"},"modified":"2012-07-29T00:33:27","modified_gmt":"2012-07-29T04:33:27","slug":"amyloid-model-peptides","status":"publish","type":"page","link":"https:\/\/www.bumc.bu.edu\/msr\/research-topics\/amyloid-model-peptides\/","title":{"rendered":"Amyloid Model Peptides"},"content":{"rendered":"<p><strong>Structural Analysis of Amyloid Model Peptides<\/strong><\/p>\n<p>Amyloid-like structure of BetaBellin Peptides<br \/>\n<img loading=\"lazy\" border=\"0\" src=\"https:\/\/www.bumc.bu.edu\/msr\/files\/Images\/JSB_cover_web.jpg\" width=\"325\" height=\"432\" alt=\"journal of structural biology cover\" \/><\/p>\n<p>This recently published cover article used a variety of techniques from polarized light microscopy and electron microscopy to circular dichroism to high resolution x-ray crystallography to show that the model Betabellin peptide has amyloidogenic properties.&nbsp; Betabellin was designed <em>ab initio<\/em> to form a beta-barrel structure, under certain conditions, this structure can be induced into a beta-pleated sheet conformation that forms fibrils in vitro.&nbsp; These fibrils show classic &#8220;apple-green&#8221; birefringence and the crystallography shows the beta-pleated sheet clearly resolving the periodicity of the folds.<\/p>\n<p>For more information, please visit the <a href=\"http:\/\/www.apnet.com\/www\/journal\/sb.htm\" target=\"blank\">Journal of Structural Biology<\/a> website , or contact <a href=\"mailto:cecmsms@bu.edu\">Cathy Costello<\/a> for reprints.&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Structural Analysis of Amyloid Model Peptides Amyloid-like structure of BetaBellin Peptides This recently published cover article used a variety of techniques from polarized light microscopy and electron microscopy to circular dichroism to high resolution x-ray crystallography to show that the model Betabellin peptide has amyloidogenic properties.&nbsp; Betabellin was designed ab initio to form a beta-barrel [&hellip;]<\/p>\n","protected":false},"author":2,"featured_media":0,"parent":6,"menu_order":22,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/pages\/24"}],"collection":[{"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/comments?post=24"}],"version-history":[{"count":1,"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/pages\/24\/revisions"}],"predecessor-version":[{"id":1641,"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/pages\/24\/revisions\/1641"}],"up":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/pages\/6"}],"wp:attachment":[{"href":"https:\/\/www.bumc.bu.edu\/msr\/wp-json\/wp\/v2\/media?parent=24"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}