📍 Venue: ICIQ Auditorium Prof. Dr. Kilian Muñiz
📅 Date: 27 November
🕙 Time: Starting at 10 a.m.
We would like to invite you to the Mini-Symposium on Protein Design, which will take place at the ICIQ Auditorium Prof. Dr. Kilian Muñiz on November 27th at 10 a.m.
Come and discover the latest advances in the fascinating world or protein engineering and design!
🕙 10 a.m – Dr. Sara H. Mejías (IMDEA Nanomaterials, Spain)
Talk title: “The relevance on amino acid-chromophore interaction in protein conformational changes and their impact on Chromophore relaxation dynamics”
Abstract:
In natural photosynthesis, light energy is transferred through a dynamic protein-pigment network with remarkably high quantum efficiency. Local fluctuations in protein structure and conformational changes play a crucial role in shaping the chromophore’s energy landscape for efficient light harvesting. However, the precise mechanistic role of these conformational changes remains unclear due to the complexity of natural photosystems, making them difficult to control. Photoactive biohybrids (Fig.1)—synthetic systems that incorporate the key components of natural photosystems, such as proteins and chromophores—offer a promising approach for applying these natural principles in man-made technologies. However, designing these biohybrids presents significant challenges, particularly in controlling the protein-chromophore interaction network, which unpredictably affects the electronic and conformational states of the chromophores. In our lab, we have developed biohybrids based on optimized de novo proteins with well-defined cavities and flexible conformational states. This design enables precise tuning of the biohybrid’s response through single-point mutations. Our biohybrids provide a powerful platform for studying the fundamental role of protein amino acids in chromophore relaxation, offering new insights for bio-inspired nanotechnology and photonics.
🕙 11 a.m – Dr. Bruce Lichtenstein (University of Portsmouth, United Kingdom)
Talk title: “Engineering and design to characterise and improve the function of polymer degrading enzymes for industrial applications”
Abstract:
Plastics are foundational to modern society, yet their durability has made them persistent environmental pollutants. Derived largely from petroleum feedstocks, these synthetic polymers contribute significantly to linear carbon economies and pose growing risks to environmental and human health. Engineered enzymes offer a promising biological solution for plastic deconstruction, enabling low-energy, sustainable methods to recycle and upcycle plastic waste — ultimately decoupling plastic life cycles from fossil fuels and greenhouse gas emissions.
Our research focuses on understanding the physical parameters that govern enzyme activity on synthetic materials. We use protein design and engineering both to probe mechanistic details and to enhance enzyme performance for plastic deconstruction, with a particular emphasis on polyethylene terephthalate (PET). We have elucidated the basis of a previously unexplained and undesirable concentration-dependent autoinhibition of PET-degrading enzymes at solid surfaces[1]. More recently, we uncovered the critical role of protein–polymer electrostatic matching in determining enzyme morphological preferences, and for the first time, identified a mechanism enabling synergistic enzymatic activity on PET films[2].
Together, these findings uncover key molecular features that govern enzyme efficiency and specificity in the context of plastic degradation. They not only inform rational strategies for enzyme engineering but also provide design principles for developing effective biological solutions to plastic pollution.
Don’t miss this opportunity to engage with leading researchers and explore cutting-edge approaches in protein design!
Join our team to work with renowned researchers, tackle groundbreaking
projects and contribute to meaningful scientific advancements