In this talk I will present two aspects of framework studies within my group. Firstly, I will discuss rational search for zeolites among hypothetical structures, and secondly, development of novel methods for protein thermal stability.
Today synthetic zeolites are the most important catalysts in petrochemical refineries because of their high internal surface areas and catalytic and chemical properties. There have been considerable efforts to synthesize new zeolites with specific pore geometries, to add to 217 available at present. Millions of hypothetical structures have been generated on the basis of energy minimization, and there is an on-going search for criteria capable of predicting new zeolite structures. We have recently discovered a new property of realizable zeolites – the flexibility window – which is a theoretical measure which can provide a valuable selection criterion when evaluating hypothetical zeolite framework structures as potential synthetic targets. I will show that the flexibility window is a necessary structural feature that enables zeolite synthesis.
Another area is use of silica to make biological proteins stable at room temperature. Most vaccines, antibodies, antiviral drugs are not stable at room temperature; they degrade over time and lose their potency. Cold chain costs more than vaccines in some areas of the world and problems in cold chain can lead to inactive vaccine administration. We have been developing methods for making proteins stable for transport and storage with no cold chain. Here, we use silica to encase the proteins, which prevents their physical unfolding and thus denaturation. I will show some latest results we have obtained on three proteins and will discuss some possible routes for the future work.
Google’s Solve for <X> conference link to my talk: