An efficient route to either enantiomer of trans-2-aminocyclopentanecarboxylic acid.
An efficient route to either enantiomer of trans-2-aminocyclopentanecarboxylic acid.
复制标题
获得反式-2-氨基环戊烷甲酸任一对映体的有效途径。
DOI：
10.1021/jo010279h
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Gellman,SH
中科院分区：
文献类型：
--
作者：
LePlae,PR;Umezawa,N;Lee,HS;Gellman,SH
Oligomers of β-amino acids (β-peptides) can be designed to adopt a variety of secondary structures, helix, sheet, or turn, by proper choice of residue substitution pattern. 1 β-Peptide helices have proven to be very stable conformationally, with oligomers containing as few as six residues displaying high helix populations in aqueous solution. 2 The predictability and stability of β-peptide conformations have led recently to the design of specific β-peptides with useful biological activities. 3 Further exploration of β-peptide function will be facilitated by improvements in the synthesis of the requisite β-amino acids. 4We have shown that oligomers composed of trans-2-aminocyclopentanecarboxylic acid (ACPC) adopt a helical conformation that contains a network of 12-membered ring hydrogen bonds between backbone CdO and NH groups (12-helix). 5 Use of a pyrrolidine-based analogue of ACPC allowed us to generate short water-soluble β-peptides and to demonstrate that these oligomers fold to the 12-helix in aqueous solution. 2 We have recently shown that an ACPC-containing β-peptide displays interesting antibiotic activity. 3c The synthesis of protected ACPC derivatives we originally employed5 was serviceable for moderate quantities of only the R, R enantiomer. Here, we report a more efficient synthesis of ACPC derivatives that gives access to either enantiomeric series in large quantities (> 20 g).
