Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics
Oligomers which have a tendency to form well-defined secondary structures are called foldamers. They offer an attractive opportunity for the design of novel molecules that mimic the structures and functions of proteins and enzymes including biocatalysis and biomolecular recognition. Herein a new cla...
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| Format: | Others |
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Scholar Commons
2015
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| Online Access: | https://scholarcommons.usf.edu/etd/5762 https://scholarcommons.usf.edu/cgi/viewcontent.cgi?article=6960&context=etd |
| Summary: | Oligomers which have a tendency to form well-defined secondary structures are called foldamers. They offer an attractive opportunity for the design of novel molecules that mimic the structures and functions of proteins and enzymes including biocatalysis and biomolecular recognition. Herein a new class of non-natural γ-AApeptides and their derivatives are synthesized and studied in our lab. Previous studies of γ-AApeptides have revealed that they are highly resistant to proteolysis, and have virtually limitless potential in functional group diversity. However, to improve the bio-activity and explore new bio-applications, the understanding of the folding conformation of γ-AApeptides are necessary. Thus, NMR spectroscopy is used to interpret the 3D structures of these γ-AApeptides. The two-dimensional solution NMR spectroscopy data for those sequences demonstrate right-handed helical structures. Further development of γ-AApeptide may lead to new foldamers with discrete functions, enabling expanded application in chemical biology and biomedical sciences. |
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