From fdade490ad65feb06f22c3329ae644631538c8ce Mon Sep 17 00:00:00 2001
From: KianBV <91744358+KianBV@users.noreply.github.com>
Date: Mon, 7 Oct 2024 14:07:30 +0200
Subject: [PATCH] Update index.md

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-# iDEC 2024 | Evolution Suisse
+---
+hide:
+  - navigation
+---
 
-This wiki template was built using [Material for MkDocs](https://squidfunk.github.io/mkdocs-material/). You are by no means confined to use this template. In fact, you are encouraged to build your own unique **static site** that best suits your project, and you are free to use any framework you like.
 
-Should you decide to use this wiki, however, we have a [tutorial](https://wiki.idec.io/team_wiki/mkdocs/) to walk you through the basics.
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+# Developing novel Targeted Protein Pegradation strategies using Directed Evolution
+
+## The Challenge
+
+Diseases caused by the accumulation of excess or misfolded proteins or their unintended overactivity, such as Alzheimer's, Parkinson's, Huntington's disease, and certain cancers, pose a significant challenge in medicine. These conditions are often characterised by toxic protein aggregates or chronically active proteins that disrupt normal cellular functions, lead to cell death, and trigger chronic inflammation. Targeted Protein Degradation (TPD) has emerged as an exciting new therapeutic approach to combat these diseases by targeting and eliminating the problematic proteins that drive their progression. Unlike current TPD strategies, which can inadvertently affect healthy proteins, cause toxicity, or miss their intended targets, we aim to develop a more precise method of TPD that specifically targets disease-associated proteins while minimising off-target effects and toxicity. 
+
+The body naturally disposes of damaged proteins through a system known as the Ubiquitin-Proteasome System (UPS). In this system, damaged or excess proteins are tagged with ubiquitin, a small protein that signals the cell’s machinery to degrade the tagged proteins. The proteasome, a cellular complex, then breaks down these proteins into harmless components. By leveraging this natural process, TPD offers a powerful strategy to selectively eliminate disease-associated proteins, offering the potential for more effective treatments with fewer side effects on healthy tissues.
+
+## Our Approach
+
+We are developing a novel approach that exploits the ability of the UPS to more effectively target proteins for degradation. Our strategy focuses on reprogramming a key player of this system, the E3 ubiquitin ligase, to selectively recognise and degrade harmful proteins associated with disease. Using directed evolution, a powerful technique that mimics natural selection in the laboratory, we aim to engineer E3 ligases capable of targeting specific disease-causing proteins. By engineering these ligases to recognise specific substrates, we are working towards a platform that can rapidly produce customised ligases with precise recognition and degradation capabilities, providing a new avenue to treat diseases. 
+
+
+## Our Workflow
+
+## Key achievements:
+
+## References