Publications by authors named "D W Calabrese"
Article Synopsis
- A better understanding of chronic lung allograft dysfunction (CLAD) is needed, as it leads to high mortality rates after lung transplants.
- The study focused on a genetic variation (C3R102G) that enhances complement activation, finding that lung transplant recipients with this variation tend to have poorer outcomes related to CLAD, especially if they develop donor-specific antibodies.
- In experiments with mice, decreased regulation of the complement system resulted in worse airway damage and increased B cell activity, linking genetic predisposition to complement activation with worse survival outcomes after lung transplantation.
An approach is described for high-throughput quality assessment of drug candidate libraries using high-resolution acoustic ejection mass spectrometry (AEMS). Sample introduction from 1536-well plates is demonstrated for this application using 2.5 nL acoustically dispensed sample droplets into an Open Port Interface (OPI) with pneumatically assisted electrospray ionization at a rate of one second per sample.
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- Imine reductases (IREDs) are valuable for synthesizing chiral amines, with applications in asymmetric imine reduction and reductive aminations of aldehydes and ketones.
- The study discusses the reductive amination of various carbonyls and dicarbonyls using hydrazines, facilitated by the IRED from Myxococcus stipitatus.
- A hydrogenase cofactor regeneration system was incorporated to enhance scalability and efficiency of the process, showcasing the significant potential of IREDs in biocatalysis.
Despite the increasing demand for efficient and sustainable chemical processes, the development of scalable systems using biocatalysis for fine chemical production remains a significant challenge. We have developed a scalable flow system using immobilized enzymes to facilitate flavin-dependent biocatalysis, targeting as a proof-of-concept asymmetric alkene reduction. The system integrates a flavin-dependent Old Yellow Enzyme (OYE) and a soluble hydrogenase to enable H-driven regeneration of the OYE cofactor FMNH.
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