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Bio-Based Elastomer Synthesis

A novel family of bio-based BDIS polyamides with tunable properties are synthesized, and the chemical structures and aggregate structures of BDISs can be tuned by simply varying the initial monomer feed ratio.

 

This new bio-based polymer exhibits versatility in mechanical properties and hydration as determined by the micro-structure of the polyamides. They can behave like semicrystalline polymer, glassy polymer and even rubbery polymer after hydration. Some of them could even be dissolved in ethonal which could endow them with safe solution processability.

 

These BDIS polyamides exhibit good in vitro cytotoxicity profiles. 

New Natural Product Methodologies

Modern structure determination of small molecules still remains a challenging problem. The number of structural reassignments reported each year is testimony to the myriad of potential pitfalls. While classical approaches to structure determination rely heavily on chemical degradation, most modern approaches use non-destructive techniques to provide the same connectivity information. Any structure determination encompasses three discrete assignments: planar, relative and absolute. Advances in NMR instrumentation and NMR pulse sequences have greatly simplified the assignment of the planar structure, i.e., the constitutional connectivity’s between the various nuclei. Conversely, relative and absolute stereochemical assignments are becoming more challenging as the isolation of submicromolar quantities of metabolites becomes increasingly more common. Consequently, my group focuses on developing new methodologies for stereochemical determinations on small scale.

Artificial beta-Sheets Peptides Synthesis

One set of projects focuses on developing molecules that mimic the folding and interaction of protein beta-sheets. Beta-Sheets are nearly ubiquitous features of proteins that consist of extended peptide strands that held together in part by a network of hydrogen bonds.

A particularly exciting and important feature of beta-sheets is their ability to interact by means of the unsatisfied hydrogen-bonding valences along their edges. Interactions between the edges of beta-sheets occur widely in proteins and are involved in both normal protein function and in diseases ranging from cancer and AIDs to Alzheimer's and Huntington's disease. Our research group has developed unnatural amino acids such as "Hao" (shown below) that induce mimic the hydrogen-bonding properties of beta-sheets and induce beta-sheet structure and interactions when incorporated into peptides. By studying the structure and interactions of peptides containing unnatural amino acids such as "Hao", we hope to gain insight into beta-sheet interactions between proteins and develop new treatments for diseases.


 

 

 

 

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