Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples
Polyproline II helix (PPII) is one of the secondary structures in proteins that play an important role in various biological processes. In this study, we have developed a new macrocyclization strategy that efficiently reinforces a model tetrapeptide into a PPII structure. We also elucidated some rel...
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ACS Publications
2020
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| Truy cập trực tuyến: | https://pubs.acs.org/doi/10.1021/acs.orglett.0c02914 https://dlib.phenikaa-uni.edu.vn/handle/PNK/586 https://doi.org/10.1021/acs.orglett.0c02914 |
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oai:localhost:PNK-5862022-08-17T05:54:38Z Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples Huy X. Luong Young-Woo Kim Peptides and proteins Circular dichroism spectroscopy, Chemical structure Metathesis Nucleic acid structure Polyproline II helix (PPII) is one of the secondary structures in proteins that play an important role in various biological processes. In this study, we have developed a new macrocyclization strategy that efficiently reinforces a model tetrapeptide into a PPII structure. We also elucidated some relationships between structural features and PPII stability in this model. This new macrocyclic stapling strategy can serve as a useful chemical tool to manipulate the PPII structure for various applications. 2020-10-13T04:18:12Z 2020-10-13T04:18:12Z 2020 Article Working Paper https://pubs.acs.org/doi/10.1021/acs.orglett.0c02914 https://dlib.phenikaa-uni.edu.vn/handle/PNK/586 https://doi.org/10.1021/acs.orglett.0c02914 en application/pdf ACS Publications |
| institution |
Digital Phenikaa |
| collection |
Digital Phenikaa |
| language |
English |
| topic |
Peptides and proteins Circular dichroism spectroscopy, Chemical structure Metathesis Nucleic acid structure |
| spellingShingle |
Peptides and proteins Circular dichroism spectroscopy, Chemical structure Metathesis Nucleic acid structure Huy X. Luong Young-Woo Kim Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples |
| description |
Polyproline II helix (PPII) is one of the secondary structures in proteins that play an important role in various biological processes. In this study, we have developed a new macrocyclization strategy that efficiently reinforces a model tetrapeptide into a PPII structure. We also elucidated some relationships between structural features and PPII stability in this model. This new macrocyclic stapling strategy can serve as a useful chemical tool to manipulate the PPII structure for various applications. |
| format |
Article |
| author |
Huy X. Luong Young-Woo Kim |
| author_facet |
Huy X. Luong Young-Woo Kim |
| author_sort |
Huy X. Luong |
| title |
Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples |
| title_short |
Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples |
| title_full |
Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples |
| title_fullStr |
Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples |
| title_full_unstemmed |
Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples |
| title_sort |
stabilization of single turn polyproline ii helices via macrocyclic hydrocarbon staples |
| publisher |
ACS Publications |
| publishDate |
2020 |
| url |
https://pubs.acs.org/doi/10.1021/acs.orglett.0c02914 https://dlib.phenikaa-uni.edu.vn/handle/PNK/586 https://doi.org/10.1021/acs.orglett.0c02914 |
| _version_ |
1751856316203139072 |
| score |
8.891787 |