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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ndltd-USF-oai-scholarcommons.usf.edu-etd-69602019-10-04T05:07:12Z Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics Qiao, Qiao 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. 2015-09-16T20:51:59Z text application/pdf https://scholarcommons.usf.edu/etd/5762 https://scholarcommons.usf.edu/cgi/viewcontent.cgi?article=6960&context=etd default Graduate Theses and Dissertations Scholar Commons NMR structure NOE stоchаstic dynаmics Chemistry |
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NMR structure NOE stоchаstic dynаmics Chemistry Qiao, Qiao Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics |
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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. |
author |
Qiao, Qiao |
author_facet |
Qiao, Qiao |
author_sort |
Qiao, Qiao |
title |
Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics |
title_short |
Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics |
title_full |
Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics |
title_fullStr |
Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics |
title_full_unstemmed |
Investigаtiоn оf 3D Structures оf γ-AAрeрtide bаsed Peрtidоmimetics |
title_sort |
investigаtiоn оf 3d structures оf γ-aaрeрtide bаsed peрtidоmimetics |
publisher |
Scholar Commons |
publishDate |
2015 |
url |
https://scholarcommons.usf.edu/etd/5762 https://scholarcommons.usf.edu/cgi/viewcontent.cgi?article=6960&context=etd |
work_keys_str_mv |
AT qiaoqiao investigationof3dstructuresofgaarertidebasedpertidomimetics |
_version_ |
1719260253675061248 |