Helical α/β-depsipeptides with alternating residue types: Conformational change from the 11-helix to the 14/15-helix

Jaeyeon Lee; Geunhyeok Jang; Philjae Kang; Moon Gun Choi; Soo Hyuk Choi

doi:10.1039/c6ob01602b

Helical α/β-depsipeptides with alternating residue types: Conformational change from the 11-helix to the 14/15-helix

Jaeyeon Lee, Geunhyeok Jang, Philjae Kang, Moon Gun Choi, Soo Hyuk Choi

Department of Chemistry

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

1 Citation (Scopus)

Abstract

Short α/β-peptides that consist of alternating l-α-amino acids and trans-2-aminocyclopentanecarboxylic acid are known to adopt both 11- and 14/15-helical conformations in solution. We report short α/β-depsipeptides containing (S)-lactic acid as the third residue from the N-terminus. The α/β-depsipeptide pentamers and heptamers adopt 14/15-helical conformations analogous to the α-helix in the crystal state and display 14/15-helical conformations predominantly in solution.

Original language	English
Pages (from-to)	8438-8442
Number of pages	5
Journal	Organic and Biomolecular Chemistry
Volume	14
Issue number	36
DOIs	https://doi.org/10.1039/c6ob01602b
Publication status	Published - 2016

Bibliographical note

Publisher Copyright:
© 2014 The Royal Society of Chemistry.

All Science Journal Classification (ASJC) codes

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1039/c6ob01602b

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title = "Helical α/β-depsipeptides with alternating residue types: Conformational change from the 11-helix to the 14/15-helix",

abstract = "Short α/β-peptides that consist of alternating l-α-amino acids and trans-2-aminocyclopentanecarboxylic acid are known to adopt both 11- and 14/15-helical conformations in solution. We report short α/β-depsipeptides containing (S)-lactic acid as the third residue from the N-terminus. The α/β-depsipeptide pentamers and heptamers adopt 14/15-helical conformations analogous to the α-helix in the crystal state and display 14/15-helical conformations predominantly in solution.",

author = "Jaeyeon Lee and Geunhyeok Jang and Philjae Kang and Choi, {Moon Gun} and Choi, {Soo Hyuk}",

note = "Publisher Copyright: {\textcopyright} 2014 The Royal Society of Chemistry.",

year = "2016",

doi = "10.1039/c6ob01602b",

language = "English",

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pages = "8438--8442",

journal = "Organic and Biomolecular Chemistry",

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T2 - Conformational change from the 11-helix to the 14/15-helix

AU - Lee, Jaeyeon

AU - Jang, Geunhyeok

AU - Kang, Philjae

AU - Choi, Moon Gun

AU - Choi, Soo Hyuk

PY - 2016

Y1 - 2016

N2 - Short α/β-peptides that consist of alternating l-α-amino acids and trans-2-aminocyclopentanecarboxylic acid are known to adopt both 11- and 14/15-helical conformations in solution. We report short α/β-depsipeptides containing (S)-lactic acid as the third residue from the N-terminus. The α/β-depsipeptide pentamers and heptamers adopt 14/15-helical conformations analogous to the α-helix in the crystal state and display 14/15-helical conformations predominantly in solution.

AB - Short α/β-peptides that consist of alternating l-α-amino acids and trans-2-aminocyclopentanecarboxylic acid are known to adopt both 11- and 14/15-helical conformations in solution. We report short α/β-depsipeptides containing (S)-lactic acid as the third residue from the N-terminus. The α/β-depsipeptide pentamers and heptamers adopt 14/15-helical conformations analogous to the α-helix in the crystal state and display 14/15-helical conformations predominantly in solution.

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JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

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ER -

Helical α/β-depsipeptides with alternating residue types: Conformational change from the 11-helix to the 14/15-helix

Abstract

Bibliographical note

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