Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples

Huy X. Luong; Young Woo Kim

doi:10.1021/acs.orglett.0c02914

Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples

Huy X. Luong
, Young Woo Kim

Department of Pharmacy

Dongguk University

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	7986-7990
Number of pages	5
Journal	Organic Letters
Volume	22
Issue number	20
DOIs	https://doi.org/10.1021/acs.orglett.0c02914
State	Published - 16 Oct 2020

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title = "Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples",

abstract = "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.",

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AU - Luong, Huy X.

AU - Kim, Young Woo

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N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85093539476

U2 - 10.1021/acs.orglett.0c02914

DO - 10.1021/acs.orglett.0c02914

M3 - Article

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AN - SCOPUS:85093539476

SN - 1523-7060

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SP - 7986

EP - 7990

JO - Organic Letters

JF - Organic Letters

IS - 20

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Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples

Abstract

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