{"id":2715,"date":"2020-02-12T15:18:06","date_gmt":"2020-02-12T14:18:06","guid":{"rendered":"https:\/\/ibb.uab.cat\/?p=2715"},"modified":"2020-03-02T08:42:54","modified_gmt":"2020-03-02T07:42:54","slug":"dra-neus-ferrer-aggregation-prone-peptides-modulate-activity-of-bovine-interferon-gamma-released-from-naturally-occurring-protein-nanoparticles","status":"publish","type":"post","link":"https:\/\/ibb.uab.cat\/index.php\/2020\/02\/12\/dra-neus-ferrer-aggregation-prone-peptides-modulate-activity-of-bovine-interferon-gamma-released-from-naturally-occurring-protein-nanoparticles\/","title":{"rendered":"Dra. Neus Ferrer-Miralles: Aggregation-prone peptides modulate activity of bovine interferon gamma released from naturally occurring protein nanoparticles"},"content":{"rendered":"<h2 class=\"section-title u-h3 u-margin-l-top u-margin-xs-bottom\"><img loading=\"lazy\" class=\" wp-image-2777 alignleft\" src=\"https:\/\/ibb.uab.cat\/wp-content\/uploads\/Figura-1-JoVi1.jpg\" alt=\"\" width=\"789\" height=\"444\" srcset=\"https:\/\/ibb.uab.cat\/wp-content\/uploads\/Figura-1-JoVi1.jpg 1280w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/Figura-1-JoVi1-300x169.jpg 300w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/Figura-1-JoVi1-768x432.jpg 768w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/Figura-1-JoVi1-1024x576.jpg 1024w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/Figura-1-JoVi1-462x260.jpg 462w\" sizes=\"(max-width: 789px) 100vw, 789px\" \/><\/h2>\n<h2><span style=\"font-size: 12pt;\">https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1871678419302134?dgcid=coauthor<\/span><\/h2>\n<h2>https:\/\/doi.org\/10.1016\/j.nbt.2020.02.001<\/h2>\n<h2 class=\"section-title u-h3 u-margin-l-top u-margin-xs-bottom\">Abstract<\/h2>\n<div id=\"abst0010\">\n<p id=\"spar0040\" style=\"text-align: justify;\">Efficient protocols for the production of recombinant proteins are indispensable for the development of the biopharmaceutical sector. Accumulation of recombinant proteins in naturally-occurring protein aggregates is detrimental to biopharmaceutical development. In recent years, the view of protein aggregates has changed with the recognition that they are a valuable source of functional recombinant proteins. In this study, bovine interferon-gamma (rBoIFN-\u03b3) was engineered to enhance the formation of protein aggregates, also known as protein nanoparticles (NPs), by the addition of aggregation-prone peptides (APPs) in the generally recognized as safe (GRAS) bacterial\u00a0<em>Lactococcus lactis<\/em>\u00a0expression system. The L6K2, HALRU and CYOB peptides were selected to assess their intrinsic aggregation capability to nucleate protein aggregation. These APPs enhanced the tendency of the resulting protein to aggregate at the expense of total protein yield. However, fine physico-chemical characterization of the resulting intracellular protein NPs, the protein released from them and the protein purified from the soluble cell fraction indicated that the compactability of protein conformations was directly related to the biological activity of variants of IFN-\u03b3, used here as a model protein with therapeutic potential. APPs enhanced the aggregation tendency of fused rBoIFN-\u03b3 while increasing compactability of protein species. Biological activity of rBoIFN-\u03b3 was favored in more compacted conformations. Naturally-occurring protein aggregates can be produced in GRAS microorganisms as protein depots of releasable active protein. The addition of APPs to enhance the aggregation tendency has a positive impact in overall compactability and functionality of resulting protein conformers.<\/p>\n<\/div>\n<p>This work was performed in collaboration with Dr. Elena Garcia-Fruit\u00f3s research group at the IRTA and supported by grants from Instituto Nacional de Investigaci\u00f3n y Tecnolog\u00eda Agraria y Alimentaria (INIA), Ministerio de Econom\u00eda y Competitividad (MINECO), Spain to N.F.M. and E.G.F. (RTA2015-00064-C02-02 and RTA2015-00064-C02-01)<\/p>\n","protected":false},"excerpt":{"rendered":"<p>https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1871678419302134?dgcid=coauthor https:\/\/doi.org\/10.1016\/j.nbt.2020.02.001 Abstract Efficient protocols for the production of recombinant proteins are indispensable for the development of the biopharmaceutical sector. Accumulation of recombinant proteins in naturally-occurring protein aggregates is detrimental to biopharmaceutical development. In recent years, the view of protein aggregates has changed with the recognition that they are a valuable source of functional recombinant [&hellip;]<\/p>\n","protected":false},"author":65,"featured_media":2717,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[4],"tags":[],"_links":{"self":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/2715"}],"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=2715"}],"version-history":[{"count":3,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/2715\/revisions"}],"predecessor-version":[{"id":2778,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/2715\/revisions\/2778"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media\/2717"}],"wp:attachment":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media?parent=2715"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/categories?post=2715"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/tags?post=2715"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}