Synthesis and conformational analysis of an anti ‐β 2, 3 ‐amino acid as a building block for unnatural peptide helices
Abstract Anti ‐β 2,3 ‐amino acids are a class of acyclic β‐amino acids that usually stabilize β‐sheet‐like conformations of unnatural peptides. (2 S ,3 R )‐3‐amino‐2‐ethylpentanoic acid (AEPA) is a diethyl‐substituted anti ‐β 2,3 ‐amino acid that can be regarded as an acyclic analog of cis ‐2‐aminoc...
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| Published in | Bulletin of the Korean Chemical Society Vol. 43; no. 2; pp. 241 - 245 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
01.02.2022
|
| Online Access | Get full text |
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| Summary: | Abstract
Anti
‐β
2,3
‐amino acids are a class of acyclic β‐amino acids that usually stabilize β‐sheet‐like conformations of unnatural peptides. (2
S
,3
R
)‐3‐amino‐2‐ethylpentanoic acid (AEPA) is a diethyl‐substituted
anti
‐β
2,3
‐amino acid that can be regarded as an acyclic analog of
cis
‐2‐aminocyclohexanecarboxylic acid, which is known to promote the α/β‐peptide 11/9‐helix and the β‐peptide 12/10‐helix. We report that AEPA can be incorporated into the two unnatural peptide helices without disrupting helical folding. Crystal structure data reveal that the
anti
‐β
2,3
‐residue adopts unconventional
gauche
(+) conformation in those unnatural peptide helices. |
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| ISSN: | 1229-5949 1229-5949 |
| DOI: | 10.1002/bkcs.12457 |