Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents

Mihye Lee; Jihyun Shim; Philjae Kang; Moon Gun Choi; Soo Hyuk Choi

doi:10.1039/c6cc01189f

Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents

Mihye Lee, Jihyun Shim, Philjae Kang, Moon Gun Choi, Soo Hyuk Choi

Department of Chemistry

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

6 Citations (Scopus)

Abstract

α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.

Original language	English
Pages (from-to)	5950-5952
Number of pages	3
Journal	Chemical Communications
Volume	52
Issue number	35
DOIs	https://doi.org/10.1039/c6cc01189f
Publication status	Published - 2016 May 1

Bibliographical note

Funding Information:
This study was supported by the Basic Science Research Program (NRF-2014R1A1A2053841) and the BK21 plus program through the National Research Foundation of Korea.

All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c6cc01189f

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title = "Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents",

abstract = "α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.",

author = "Mihye Lee and Jihyun Shim and Philjae Kang and Choi, {Moon Gun} and Choi, {Soo Hyuk}",

note = "Funding Information: This study was supported by the Basic Science Research Program (NRF-2014R1A1A2053841) and the BK21 plus program through the National Research Foundation of Korea.",

year = "2016",

month = may,

day = "1",

doi = "10.1039/c6cc01189f",

language = "English",

volume = "52",

pages = "5950--5952",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

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T1 - Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents

AU - Lee, Mihye

AU - Shim, Jihyun

AU - Kang, Philjae

AU - Choi, Moon Gun

AU - Choi, Soo Hyuk

N1 - Funding Information: This study was supported by the Basic Science Research Program (NRF-2014R1A1A2053841) and the BK21 plus program through the National Research Foundation of Korea.

PY - 2016/5/1

Y1 - 2016/5/1

N2 - α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.

AB - α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.

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