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Solving the puzzle of polymer-ice binding for cryopreservation

When biological material is frozen, cryoprotectants are used to prevent ice damage. How do newly emerging polymeric cryoprotectants control ice formation and growth during freezing?

Soil bacteria hormone discovery provides fertile ground for new antibiotics

The discovery of how hormone-like molecules turn on antibiotic production in soil bacteria could unlock the untapped opportunities for medicines that are under our very feet.

An international team of scientists working in the Department of Chemistry, the School of Life Sciences and the Warwick Integrative Synthetic Biology Centre at the University of Warwick, UK, and Monash University, Australia, have determined the molecular basis of a biological mechanism that could enable more efficient and cost-effective production of existing antibiotics, and also allow scientists to uncover new antibiotics in soil bacteria.

It is detailed in a new study published in the journal Nature.

Thu 11 Feb 2021, 08:23 | Tags: publications ChemBio Research news

New company, CryoLogyx, is spun out from the Department

A new biotechnology company, CryoLogyx, has been spun-out from the department, supported from a grant from InnovateUK. Cryologyx will be led by Dr Tom Congdon (A UoW UG and PG alumus) and will exploit technology developed by the GibsonGroup. Cryologyx will use innovative macromolecular (polymeric) cryoprotectants to protect biological samples, including cells used in therapy, diagnostics and drug discovery.

Read the news story here and more details will be released soon.

Wed 10 Feb 2021, 14:59 | Tags: news people MatPolymers ChemBio Impact

Dixon Group publishes first molecular description of VanS binding site within vancomycin antibiotic, offering potential in future therapeutic engineering

Resistance has emerged to vancomycin, a last-resort antibiotic for treatment of MRSA. The VanSR regulatory system induces expression of resistance genes upon exposure; however, the mechanism of vancomycin detection was unclear. Through solution NMR and other biophysical methods, we reveal a direct interaction between vancomycin and the extracellular domain of VanS from Streptomyces coelicolor. The VanS-binding epitope within vancomycin was mapped to a region distinct from the binding site for Lipid II. In targeting a separate site, the effective VanS ligand concentration includes both free and lipid-bound molecules, facilitating VanS activation. This is the first molecular description of the VanS/vancomycin interface, and could direct engineering of future therapeutics.

Tue 14 Jul 2020, 12:40 | Tags: ChemBio Research news

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