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In these changed circumstances due to COVID-19 social distancing protocols and stay at home advisory, we are trying to get fellow graduate students and Faculty together virtually to listen to interesting research talks and exchange ideas and a brainstorming session.
The first Research Talk for Summer will be presented by Kingshuk Dutta from Thai Lab on 20th May at 11 am
Title of the talk: "Self-Assembly of Stimuli-Responsive Polymers for Encapsulation and Triggered Release of Proteins"
Abstract :
Designing a supramolecular assembly that is capable of stably holding sensitive active and releasing at target site upon environmental changes is a promising solution to address complex drug delivery challenges. To this end, we have explored the interactions between synthetic polymers with biomacromolecules to form well-defined self-assembled structures. A covalent self-assembly strategy has been developed with designed polymers to reversibly capture sensitive biomacromolecules, e.g., proteins and antibodies. The rationally-designed polymer structures (i) trigger the formation of templated assemblies, (ii) protect the encapsulated active from degradation in non-native environment, (iii) can turn-off the function of active while encapsulated, and (iv) concurrently help to turn-on its function only in response to a redox stimulus upon releasing. The triggered release behaviour is achieved via structural design of stimuli-responsive polymers with activated carbonate esters. The reported strategy could provide a simple and robust drug delivery platform potentially applicable to a broad range of biologics and would help design the next generation therapeutics.
The second Research Talk for Summer will be presented by Ishankumar Soni from Hardy Lab on 22nd June at 11 am.
Title of the talk: Why Procaspase-6 Is A Poor Substrate of Caspase-9?
Abstract:
Caspases, cysteine-aspartate proteases, play a key role in apoptosis (programmed cell- death). Upon intrinsic stress, caspase-9, an apical caspase initiates apoptosis by cleaving the intersubunit linker of executioner procaspase-3 and -7. Based on our initial findings, executioner procaspase-6, also involved in neurodegenerative pathway, is not cleaved at its intersubunit linker by caspase-9. This result has prompted us to investigate protease-substrate interactions between caspase-9 and procaspase-6. Our combinatory approach of using site-directed mutagenesis and substrate digestion assays has demonstrated that both the sequence and context of procaspase-6 intersubunit linker are involved in cleavage protection by caspase-9.
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