Co-immobilization of Enzymes on Metal-Organic Frameworks
In a recent study, HRP/GOx enzyme system was immobilized on two synthetically modified MOFs, UiO-66 and UiO-66-NH2, to study the effects of immobilization and enzyme activity at the MOF interface. Learn More.
Metal-organic frameworks are coordination networks composed of organic linkers and inorganic nodes containing potential void space with large surface areas. MOFs stand out as effective solid supports for immobilization due to their highly tunable organic linkers and potential void space, which are ideal for the design of strong guest-host interactions. In many respects, enzymes offer advantages over traditional chemical processes due to their decreased energy requirements for function and inherent greener processing. However, significant barriers exist for the utilization of enzymes in industrial processes due to their limited stabilities and inability to operate over larger temperature and pH ranges.
Co-immobilization of enzymes onto solid supports has gained attention as an alternative to traditional chemical processes due to enhanced enzymatic performance and stability. We focus on utilizing tunable MOFs to co-immobilize enzymes for more effective biocatalysts.
Expression of a Lanthanide Binding Protien Lanmodulin to Investigate its Metal Binding Properties
Lanmodulin is a protein capable of selectively binding to lanthanides. It was originally discovered in the methylotroph Methylobacterium extorquens that uses lanthanides as a cofactor for methanol dehydrogenase. This protein has an EF hand binding motif similar to that of the calcium binding protein, calmodulin, but with conserved proline residues at the start of the binding sequence. There is considerable interest in discovering the mechanism of lanthanide binding to lanmodulin and insight into its incredible selectivity over calcium despite the EF hand binding motif that it shares with calmodulin. Lanmodulin can be harvested directly from M. extorquens to study, but it also can be recombinantly expressed in E. coli.
Utilizing Tyrosinase as a Model Enzyme to Explore Structure-Function Relationships Within a Research Collaboration Network
Ideating and implementing undergraduate learning opportunities that simultaneously advance research progress is challenging. Course-based Undergraduate Research Experiences (CUREs) that are nationally networked address this challenge by providing the infrastructure for faculty to plug into and easily integrate research into their classes. Design2Data (D2D) is a growing nationally-networked CURE that involves students in investigating structure-function relationships in enzymes and collecting relevant data for the computational protein modeling and design stakeholder community. One of the tasks in this network is to identify enzymes that are amenable to the already established D2D workflow. A good enzyme target must: have an available structure, express well in Escherichia coli (E. coli), utilize a colorimetric assay, and be related to human health. One target here is tyrosinase. Tyrosinase is copper-containing metalloenzyme that catalyzes the oxidation of monophenols to ortho-diphenols and ortho-quinones. Tyrosinase plays a major role in the first step of the melanogenesis process. Working with tyrosinase can be a difficult task because the commercially available product can be impure and have low activity, making tyrosinase a great candidate for recombinant studies.
Structural and Catalytic Investigation of Manganese Oxides Produced by P. putida MnB1
Manganese oxides (MnOx) are among the strongest oxidants found in the environment. Although the process of Mn(II) to Mn(IV) oxidation is thermodynamically favorable, it is a very slow process without the presence of a catalyst. Pseudomonas putida MnB1 is a Gram-negative bacteria found in both soil and freshwater. The biogenic manganese oxides formed by MnB1 deposit on the surface of the bacterial cell. Compared to abiotic manganese oxides, BMOs have poor crystallinity; despite this, BMOs have higher surface area and reactivity.
Developing MOF Agents for PDT Drug Delivery for Cancer Treatments
MOF targeting drug delivery system is able to release therapeutic compounds once they reached the diseased tissues and cells. The targeting strategy can improve the concentration of the drugs at the tumor site to improve the efficacy and avoid the release of the drugs in normal tissues. The metal organic framework (MOF) MIL-68(Al)-NH2 is being used as the drug delivery agent to the photosensitizer phycocyanin. Studies such as crystallization of phycocyanin, absorption binding, rate constants, zeta potential, and DFT will be done to observe the interaction between the physcocyanin and MIL-68(Al)-NH2. If proven that phycocyanin is being absorbed by the MOF further pH responsive studies will be done to observe the release of the photosensitizer.
Drug Discovery of Aminoacylase Inhibitors
After the FDA placed more restrictions on the testing of drugs, drug development has become costly without any discovery of drug(s). To aid this, computational drug development programs have been developed in order to aid drug research and development. Maestro, a program from Schrödinger, helps aid in this area specifically with hit identification, hit to lead identification, and lead optimization. This approach was applied to, Histone deacetylase (HDAC), which correlates to neurodegenerative diseases, is a class of enzymes that remove acetyl groups (O=C-CH3) from an ε-N-acetyl-lysine amino acid on a histone. This allows the histone groups to wrap around the DNA more tightly. Causing the DNA to be less assessable to transcription factors. Due to limited financial resources a similar compound to substitute H DAC is used. The substituted compound is aminoacylated. Both of these proteins are you zinc-dependent acylase that shares a common mechanism.
A Learning Community Involving Collaborative Course-Based Research Experiences for Foundational Chemistry Laboratories
Incorporating research experience in fundamental undergraduate courses to engage students in relevant research topics and enhance their scientific skills. Learn More.
Numerous American national committees have recommended the replacement of traditional labs with a more engaging curriculum that inspires inquiry and enhances scientific skills (examples include the President’s Council of Advisors on Science and Technology (PCAST)’s Engage to Excel program and American Association for the Advancement of Science (AAAS) Vision and Change, among others), due to a large body of evidence that shows significant enhancements in student learning and affective outcomes. The implementation of Course-Based Undergraduate Research Experiences (CUREs) is a creative way to scale up the deployment of authentic research experiences to students. Another highly regarded high-impact practice in postsecondary education is the addition of learning communities. The integration of a three-course learning community and authentic research experiences to laboratory courses adds both a community of scholarship and a development of scientific communication and process skills. This study describes a course that blends these two high-impact practices in higher education in order to promote greater post-course gains in essential elements of a CURE curriculum. This collaborative course shows large post-course gains in essential elements, such as scientific communication and working collaboratively.
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