{"id":12,"date":"2020-02-11T13:10:50","date_gmt":"2020-02-11T13:10:50","guid":{"rendered":"http:\/\/161.116.93.61\/?page_id=12"},"modified":"2025-01-17T16:17:25","modified_gmt":"2025-01-17T16:17:25","slug":"research","status":"publish","type":"page","link":"https:\/\/www.ub.edu\/tpdlab\/research\/","title":{"rendered":"Research"},"content":{"rendered":"
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1. Expanding the toolbox of E3 Ligases<\/h4>\n

Our group, in collaboration with the computational chemistry lab, is involved in the development of small-molecules that target novel E3 ubiquitin ligases in order to expand the toolbox of this protein family. E3 ubiquitin ligases are involved in the recruitment of a specific substrate protein marked to be degraded via the Ubiquitin Proteasome System, making them be very attractive candidates as drug targets. However, the development of small-molecules against E3 ligases has been rewarded with limited success, in part because modulating their activity and regulation requires targeting protein-protein interactions or allosteric sites. Small-molecules that target E3 ligases could not only be developed into chemical probes<\/strong> to elucidate the best pharmacological strategy to target a specific E3 ligase, but also serve as anchors to develop disease-specific PROTAC molecules<\/strong>.<\/p>\n

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2. Novel PROTACs for undruggable proteins<\/h4>\n

The majority of proteins are still today considered undruggable for conventional drug discovery approaches. An innovative approach that can address this situation is PROTACS (PROteolysis TArgeting Chimeric) moleculeS<\/strong>. PROTACS re-direct the intracellular degradation of any Protein of Interest (POI) by linking a ligand that binds to an E3 ligase on one side and that binds the POI on the other side. The action of PROTACS does not require a functional binding site and \u201ctheoretically\u201d exerts its catalytic function through binding to any accessible protein surface. These features support the potential value of PROTACS as a revolutionizing therapeutic tool. Moreover, PROTACS emerges as a highly specific, robust and versatile approach to complement reverse genetic tools such as RNAi, CRISPR-CAS9 and other gene knockouts in the study of protein function, as it interferes at the post-translational level. The goal of the Galdeano\u2019s Lab is to demonstrate that using PROTACS molecules, it is possible to expand the current druggable proteome<\/strong>.<\/p>\n<\/div>\n<\/div><\/div>

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3. Development of novel therapies for unmet medical needs<\/h4>\n

Our research mission is to discover novel small-molecules to provide tools for a better understanding of the biology processes, and to develop novel drugs to address unmet medical needs. To achieve this goal, we employ a multidisciplinary approach that combines biophysics, medicinal chemistry, molecular and cell biology and we work closely together with computational chemists. We are particularly strong in biophysical approaches for drug discovery<\/strong>, including DSF, SPR, ITC, ligand-based NMR and fluorescence techniques. Nowadays, biophysical methods are used extensively in hit finding (fragment-based screening<\/strong>), hit validation, in depth characterization of compound binding and lead optimization. In this line, we also have a deep knowledge of the lead optimization process<\/strong> to deliver molecules to the regulatory phase. We work on a wide breath of targets, internally and in collaborative projects.<\/p>\n<\/div>\n<\/div><\/div>

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1. Expanding the toolbox of E3 Ligases Our group, in collaboration with the computational chemistry lab, is involved in the development of small-molecules that target novel E3 ubiquitin ligases in order to expand the toolbox of this protein family. E3 ubiquitin ligases are involved in the recruitment of a specific substrate protein marked to be […]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-12","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/pages\/12","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/comments?post=12"}],"version-history":[{"count":15,"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/pages\/12\/revisions"}],"predecessor-version":[{"id":605,"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/pages\/12\/revisions\/605"}],"wp:attachment":[{"href":"https:\/\/www.ub.edu\/tpdlab\/wp-json\/wp\/v2\/media?parent=12"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}