{"id":865,"date":"2024-02-14T15:38:53","date_gmt":"2024-02-14T13:38:53","guid":{"rendered":"http:\/\/www.amyloid.bti.vu.lt\/?page_id=865"},"modified":"2025-07-21T11:56:37","modified_gmt":"2025-07-21T08:56:37","slug":"mokslas","status":"publish","type":"page","link":"http:\/\/www.amyloid.bti.vu.lt\/en\/mokslas\/","title":{"rendered":"Research"},"content":{"rendered":"<h2 class=\"wp-block-heading has-palette-color-6-background-color has-background\">Research objects<\/h2>\n\n\n\n<p class=\"has-text-align-left\">We work with the proteins which form amyloid fibrils or droplets. <\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>Amyloid fibrils<\/strong> are protein aggregates with cross-beta sheet structures. They are found during neurodegenerative disorders, cardiac diseases and cancer.<\/li>\n\n\n\n<li><strong>Protein droplets <\/strong>form during liquid-liquid phase separation, which can happen inside the cell. LLPS initiate protein aggregation, but it is also associated with several protein functions.<\/li>\n<\/ul>\n\n\n\n<figure class=\"wp-block-image aligncenter size-large\"><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"395\" src=\"http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2.png\" alt=\"Schema iliustruojanti amiloidini\u0173 baltym\u0173 agregacijos proces\u0105.\" class=\"wp-image-191\" srcset=\"http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2.png 1766w, http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2-300x116.png 300w, http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2-1024x395.png 1024w, http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2-150x58.png 150w, http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2-768x296.png 768w, http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2020\/05\/schema2-1536x592.png 1536w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption class=\"wp-element-caption\">Schematic representation of the amyloid aggregation process<\/figcaption><\/figure>\n\n\n\n<p>In our laboratory, we work with these proteins: <\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>Alzheimer's disease:<\/strong>beta-amyloid, S100A, Tau; <em>Tau<\/em> baltymas. <\/li>\n\n\n\n<li><strong>Parkinson's disease:<\/strong>alpha-synuclein; <\/li>\n\n\n\n<li><strong>Spongiform encephalopathies:<\/strong> prion proteins;<\/li>\n\n\n\n<li><strong>Amyotrophic lateral sclerosis:<\/strong>Superoxide dismutase 1 (SOD1);<strong> <\/strong><\/li>\n\n\n\n<li><strong>Other amyloidoses:<\/strong>\u00df2-microglobulin, transthyretin;<\/li>\n\n\n\n<li><strong>Model proteins:<\/strong> insulin, lysozyme; <\/li>\n\n\n\n<li><strong>Bacterial and yeast proteins:<\/strong>CsgABC, Sup35, Ure2; <\/li>\n\n\n\n<li><strong>Chaperones and regulatory proteins:<\/strong>14-3-3, Hsp, DegP; <\/li>\n<\/ul>\n\n\n\n<h2 class=\"wp-block-heading has-palette-color-6-background-color has-background\">Methodology<\/h2>\n\n\n\n<div class=\"wp-block-group is-layout-constrained wp-block-group-is-layout-constrained\">\n<ul class=\"wp-block-list\">\n<li>Gene engineering;<\/li>\n\n\n\n<li>Protein and nucleic acid electrophoresis;<\/li>\n\n\n\n<li>Production of recombinant proteins in bacteria;<\/li>\n\n\n\n<li>Chromatographic methods (e.g. ion exchange chromatography, affinity chromatography, size exclusion chromatography, high-performance liquid chromatography (HPLC)) to purify proteins and other molecules of interest;<\/li>\n\n\n\n<li>Monitoring of the amyloid aggregation process by measuring the absorption or dynamic light scattering of the solution, or the intensity of amyloid-specific dye fluorescence emission. Subsequently, we analyse aggregation kinetics using chemical kinetics tools;<\/li>\n\n\n\n<li>Infrared spectroscopy to obtain insights into the secondary structure of amyloid proteins and their aggregates;<\/li>\n\n\n\n<li>Atomic force microscopy to obtain insights into aggregate morphology and physical parameters (height, length, width, periodicity); <\/li>\n\n\n\n<li>Mass spectrometry to determine mass of the protein; <\/li>\n\n\n\n<li>Baltym\u0173 strukt\u016bros nustatymai su Cryo-EM <\/li>\n<\/ul>\n<\/div>\n\n\n\n<p><\/p>","protected":false},"excerpt":{"rendered":"<p>Tyrim\u0173 objektai M\u016bs\u0173 laboratorijoje tyriami baltymai, kurie sudaro amiloidines fibriles arba la\u0161elius. M\u016bs\u0173 laboratorijoje turime patirties su \u0161iais baltymais: Metodika<\/p>","protected":false},"author":3,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-865","page","type-page","status-publish","hentry"],"blocksy_meta":[],"rise-blocks_excerpt":"Tyrim\u0173 objektai M\u016bs\u0173 laboratorijoje tyriami baltymai, kurie sudaro amiloidines fibriles arba la\u0161elius. M\u016bs\u0173 laboratorijoje turime patirties su \u0161iais baltymais: Metodika","yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.3 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Mokslas - Amiloid\u0173 tyrimo sektorius<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"http:\/\/www.amyloid.bti.vu.lt\/en\/mokslas\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Mokslas - Amiloid\u0173 tyrimo sektorius\" \/>\n<meta property=\"og:description\" content=\"Tyrim\u0173 objektai M\u016bs\u0173 laboratorijoje tyriami baltymai, kurie sudaro amiloidines fibriles arba la\u0161elius. 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