{"id":44004,"date":"2021-11-03T19:00:00","date_gmt":"2021-11-03T18:00:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=44004"},"modified":"2024-09-28T17:46:00","modified_gmt":"2024-09-28T15:46:00","slug":"structure-of-promiscuous-protein-will-help-scientists-design-better-drugs","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/structure-of-promiscuous-protein-will-help-scientists-design-better-drugs\/","title":{"rendered":"Structure of a promiscuous protein will help scientists design better drugs"},"content":{"rendered":"\n<figure class=\"vf-figure wp-block-video\"><video style=\"max-width: 100%;\" autoplay controls preload=\"auto\" src=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/10\/PepT1-animation.mp4\" playsinline><\/video><figcaption class=\"vf-figure__caption\">The human peptide transporter PepT1 transports digested proteins from the gut into the bloodstream. PepT1 also transports many drugs, including antibiotics and antivirals. The structure of PepT1 in the image is based on the PDB entries: <a href=\"https:\/\/www.rcsb.org\/structure\/7PMW>7PMW<\/a>, <a href=\"><\/a><a href=\"https:\/\/www.ebi.ac.uk\/pdbe\/entry\/pdb\/7pmw\">7PMW<\/a>, <a href=\"https:\/\/www.ebi.ac.uk\/pdbe\/entry\/pdb\/7pmx\">7PMX<\/a>, <a href=\"https:\/\/www.ebi.ac.uk\/pdbe\/entry\/pdb\/7pmy\">7PMY<\/a> and <a href=\"https:\/\/www.ebi.ac.uk\/pdbe\/entry\/pdb\/7pn1\">7PN1<\/a>. Credit: Isabel Romero Calvo\/EMBL<\/figcaption><\/figure>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a1\"><strong>The promiscuous protein that keeps us nourished<\/strong><\/h2>\n\n\n\n<p>During digestion, the proteins we eat are broken down into tinier pieces called peptides, which consist of amino acids that our body later uses to build its own proteins. Before that happens, peptides must first be transported from the gut to the bloodstream. This task is performed by a molecule called peptide transporter 1 (PepT1), which sits in the cell membrane of the intestine wall and moves small peptides across the cell membrane.<\/p>\n\n\n\n<p>In the human body, there are around 800 transport systems dedicated to different sorts of nutrients. Most of them are very specialised. For example, certain sugar transporters can take up only one type of sugar. However, PepT1 is different \u2013 it can transport almost any type of short peptide. In the scientific jargon, this ability is referred to as \u2018promiscuity\u2019.<\/p>\n\n\n\n<p>Group Leader Christian L\u00f6w is EMBL Hamburg\u2019s expert on membrane proteins. His group, together with colleagues from the <a href=\"https:\/\/www.cssb-hamburg.de\/research\/research_groups\/marlovits_group\/index_eng.html\">Centre for Structural Systems Biology (CSSB)<\/a> and the Universit\u00e4tsklinikum Hamburg-Eppendorf (UKE), determined the molecular structures of human PepT1 and its relative PepT2, which is present mainly in the kidney for nutrient resorption. The scientists used cryo-electron microscopy, a technique in which frozen samples are imaged using electrons instead of light.<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a2\"><strong>New possibilities to improve drug design<\/strong><\/h2>\n\n\n\n<p>The promiscuity of PepT1 enables it to transport not only nutritious peptides but also various types of drugs, including certain antibiotics, antivirals, and drugs for hypertension. However, PepT1 transports drugs less efficiently than it transports many of the natural peptides. As a consequence, only a fraction of the drugs we take in end up in our bloodstream. The rest stays in the gut, which may lead to various side effects. Increasing the dosage of drugs to make up for inefficient transport is particularly dangerous in the case of antibiotics, because it may lead to the generation of antibiotic-resistant bacteria.<\/p>\n\n\n\n<p>\u201cNow that we know what the PepT1 structure looks like, it will be possible to design new drugs that exploit PepT1 to cross the gut wall much more efficiently than before,\u201d said L\u00f6w. \u201cThe structure of human PepT1 will allow us to improve drug design by making the absorption more efficient. Currently, it\u2019s almost impossible to predict whether a drug candidate can cross the gut wall via this transport system. Until now, obtaining such a drug has been very challenging. Many potentially effective drug candidates have failed in preclinical studies because they were poorly absorbed. With the help of the structural information for PepT1, some of those failed candidates could be redesigned so that they could be transported efficiently by PepT1. Similarly, many existing drugs could be modified to improve their absorption.\u201d<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a3\"><strong>Watching the transporter in stop-motion<\/strong><\/h2>\n\n\n\n<p>The molecular structure of human PepT1 is among the smallest structures determined with cryo-electron microscopy. It resembles a clamp that is open towards the inside of the gut. When a peptide binds to PepT1, the clamp closes around it and then opens to the other side of the membrane to release it. The scientists not only determined the structure of the transporter but even captured it in various states along the transport cycle.<\/p>\n\n\n\n<p>\u201cWe visualised the entire transport process in molecular detail, like in a film,\u201d said Maxime Killer, first author of the study. \u201cMembrane proteins are notoriously difficult to study, but we hope that the tricks we developed to study PepT1 will help other scientists to solve the structures of similar proteins in the future.\u201d<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Scientists at EMBL Hamburg determined the molecular structure of Peptide Transporters 1 and 2. The findings will enable developing drugs that more efficiently pass from the gut to target tissues.<\/p>\n","protected":false},"author":96,"featured_media":44014,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[775,981,579,53,461,601,616,5752,35],"embl_taxonomy":[9596,19325],"class_list":["post-44004","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-cssb","tag-drug","tag-gut","tag-hamburg","tag-low","tag-nutrition","tag-protein","tag-protein-structure","tag-structural-biology","embl_taxonomy-embl-hamburg","embl_taxonomy-low-group-visiting"],"acf":{"featured":true,"show_featured_image":true,"field_target_display":"","article_intro":"<p>Scientists at EMBL Hamburg and CSSB have determined the molecular structure of a gut protein that helps us absorb many drugs. This could help to develop drugs that reach target tissues more efficiently.<\/p>\n","related_links":false,"source_article":[{"publication_title":"PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes","publication_link":{"title":"","url":"https:\/\/www.science.org\/doi\/10.1126\/sciadv.abk3259","target":"_blank"},"publication_authors":"Killer M., et al.","publication_source":"Science Advances","publication_date":"3 November 2021","publication_doi":"10.1126\/sciadv.abk3259"}],"in_this_article":[{"heading_description":"The promiscuous protein that keeps us nourished","anchor":"#a1"},{"heading_description":"New possibilities to improve drug design","anchor":"#a2"},{"heading_description":"Watching the transporter in stop-motion","anchor":"#a3"}],"press_contact":"EMBL Generic","vf_locked":false,"field_article_language":{"value":"english","label":"English"},"article_translations":false,"languages":""},"embl_taxonomy_terms":[{"uuid":"a:3:{i:0;s:36:\"b14d3f13-5670-44fb-8970-e54dfd9c921a\";i:1;s:36:\"89e00fee-87f4-482e-a801-4c3548bb6a58\";i:2;s:36:\"613c4de5-1775-447f-af71-4b07085318e9\";}","parents":[],"name":["EMBL Hamburg"],"slug":"embl-hamburg","description":"Where &gt; All EMBL sites &gt; EMBL Hamburg"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"2dc39890-6c01-47bf-ac78-d42abdb10079\";i:2;s:36:\"ff75b8fe-d6a7-4d0e-94a4-c9c1d69ed777\";}","parents":[],"name":["L\u00f6w Group (Visiting)"],"slug":"low-group-visiting","description":"What &gt; Structural Biology (EMBL Hamburg) &gt; L\u00f6w Group (Visiting)","deprecated":true}],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Structure of a promiscuous protein will help scientists design better drugs | EMBL<\/title>\n<meta name=\"description\" content=\"Scientists at EMBL Hamburg determined the structure of PepT1. This will enable designing drugs that are more efficiently absorbed.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/structure-of-promiscuous-protein-will-help-scientists-design-better-drugs\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Structure of a promiscuous protein will help scientists design better drugs | EMBL\" \/>\n<meta property=\"og:description\" content=\"Scientists at EMBL Hamburg determined the structure of PepT1. 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