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 | |
| Publication status | Published - 2016 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry
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Helical α/β-depsipeptides with alternating residue types : Conformational change from the 11-helix to the 14/15-helix. / Lee, Jaeyeon; Jang, Geunhyeok; Kang, Philjae; Choi, Moon-Gun; Choi, Soo Hyuk.
In: Organic and Biomolecular Chemistry, Vol. 14, No. 36, 01.01.2016, p. 8438-8442.Research output: Contribution to journal › Article
TY - JOUR
T1 - Helical α/β-depsipeptides with alternating residue types
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 - 2016/1/1
Y1 - 2016/1/1
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.
UR - http://www.scopus.com/inward/record.url?scp=84988369661&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84988369661&partnerID=8YFLogxK
U2 - 10.1039/c6ob01602b
DO - 10.1039/c6ob01602b
M3 - Article
C2 - 27537109
AN - SCOPUS:84988369661
VL - 14
SP - 8438
EP - 8442
JO - Organic and Biomolecular Chemistry
JF - Organic and Biomolecular Chemistry
SN - 1477-0520
IS - 36
ER -