The CADABRA project targets antibiotic residues in wastewater, driven by the growing threat of antimicrobial resistance. It focuses on excreted antibiotics in water systems, as highlighted in Bulgaria's Yantra River due to poor wastewater regulations. The European Environmental Quality Standards Directive (EQSD) mandates action on antibiotic pollution. CADABRA's primary aim is to improve metallo-β-lactamases (VIM and NDM) for breaking down β-lactam antibiotics, employing directed evolution and computational models. The project proposes using UV spectroscopy to monitor antibiotic levels in liquid samples and explores Pichia pastoris as an alternative host for safety and cost-effectiveness. In summary, CADABRA aims to revolutionize hospital wastewater antibiotic removal with advanced techniques and biosafety measures, contributing to efficient antibiotic breakdown and reliable monitoring.
We are iGEM Bulgaria – a large and cohesive team united by the wonders of synthetic biology! With rolled up sleeves and pipettes in hand, we strive to find solutions to the world's challenges. We are ambitious bachelor's and master’s students with varied backgrounds, ready to build bridges between biology, engineering and technology. We are biological ninjas moving at a stellar pace towards a better future, leaving lasting impact in science and in your hearts!
On our educational page, you'll find engaging comic and video designed to make it easy for children to grasp the concepts of bacteria and antibiotics. This year, we've taken it a step further by creating a captivating board game that centers around the epic battle between pathogens and our body's defenses, highlighting the role of medicines in this struggle. Additionally, one of our proudest achievements this year was mentoring National Science and Mathematics High School students for the IYNT competition, where they clinched the bronze medal, solidifying our commitment to nurturing young talent.
Through the application of molecular docking techniques, we have successfully constructed a model that elucidates the intricate interaction between the antibiotic meropenem and the metallo-beta-lactamase VIM. Our strategy revolved around the targeted modification of specific amino acids within the enzyme's active site. We directed our attention to amino acids that engage with the meropenem molecule while not forming strong bonds with the zinc atoms. This approach was chosen to ensure that any changes made would not significantly disrupt the overall structure of the enzyme. Preserving the enzyme's structural integrity is crucial to avoid adverse impacts on its functionality.
