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Solid-state conformations of linear depsipeptide amides with an alternating sequence of $a,a$-disubstituted $a$-amino acid and $a$-hydroxy acid


Linden, A; Magirius, J E Florian; Heimgartner, Heinz (2020). Solid-state conformations of linear depsipeptide amides with an alternating sequence of $a,a$-disubstituted $a$-amino acid and $a$-hydroxy acid. Acta Crystallographica. Section C: Structural Chemistry, C76:1-9.

Abstract

Depsipeptides and cyclodepsipeptides are analogues of the corresponding peptides in which one or more amide groups are replaced by ester functions. Reports of crystal structures of linear depsipeptides are rare. The crystal structures and conformational analyses of four depsipeptides with an alternating sequence of an alpha,alpha-disubstituted alpha-amino acid and an alpha-hydroxy acid are reported. The molecules in the linear hexadepsipeptide amide in (S)-Pms-Acp- (S)-Pms-Acp-(S)-Pms-Acp-NMe2 acetonitrile solvate, C47H58N4O9.C2H3N, (3b), as well as in the related linear tetradepsipeptide amide (S)-Pms-Aib-(S)-Pms- Aib-NMe2, C28H37N3O6, (5a), the diastereoisomeric mixture (S,R)-Pms-Acp- (R,S)-Pms-Acp-NMe2/(R,S)-Pms-Acp-(R,S)-Pms-Acp-NMe2 (1:1), C32H41N3O6, (5b), and (R,S)-Mns-Acp-(S,R)-Mns-Acp-NMe2, C30H37N3O6, (5c) (Pms is phenyllactic acid, Acp is 1-aminocyclopentanecarboxylic acid and Mns is mandelic acid), generally adopt a beta-turn conformation in the solid state, which is stabilized by intramolecular N—H...O hydrogen bonds. Whereas beta-turns of type I (or I') are formed in the cases of (3b), (5a) and (5b), which contain phenyllactic acid, the torsion angles for (5c), which incorporates mandelic acid, indicate a beta-turn in between type I and type III. Intermolecular N—H...O and O—H...O hydrogen bonds link the molecules of (3a) and (5b) into extended chains, and those of (5a) and (5c) into two-dimensional networks.

Abstract

Depsipeptides and cyclodepsipeptides are analogues of the corresponding peptides in which one or more amide groups are replaced by ester functions. Reports of crystal structures of linear depsipeptides are rare. The crystal structures and conformational analyses of four depsipeptides with an alternating sequence of an alpha,alpha-disubstituted alpha-amino acid and an alpha-hydroxy acid are reported. The molecules in the linear hexadepsipeptide amide in (S)-Pms-Acp- (S)-Pms-Acp-(S)-Pms-Acp-NMe2 acetonitrile solvate, C47H58N4O9.C2H3N, (3b), as well as in the related linear tetradepsipeptide amide (S)-Pms-Aib-(S)-Pms- Aib-NMe2, C28H37N3O6, (5a), the diastereoisomeric mixture (S,R)-Pms-Acp- (R,S)-Pms-Acp-NMe2/(R,S)-Pms-Acp-(R,S)-Pms-Acp-NMe2 (1:1), C32H41N3O6, (5b), and (R,S)-Mns-Acp-(S,R)-Mns-Acp-NMe2, C30H37N3O6, (5c) (Pms is phenyllactic acid, Acp is 1-aminocyclopentanecarboxylic acid and Mns is mandelic acid), generally adopt a beta-turn conformation in the solid state, which is stabilized by intramolecular N—H...O hydrogen bonds. Whereas beta-turns of type I (or I') are formed in the cases of (3b), (5a) and (5b), which contain phenyllactic acid, the torsion angles for (5c), which incorporates mandelic acid, indicate a beta-turn in between type I and type III. Intermolecular N—H...O and O—H...O hydrogen bonds link the molecules of (3a) and (5b) into extended chains, and those of (5a) and (5c) into two-dimensional networks.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:9 December 2020
Deposited On:09 Jan 2020 09:30
Last Modified:21 Jan 2020 04:15
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:2053-2296
OA Status:Green
Publisher DOI:https://doi.org/10.1107/S2053229619016073
Project Information:
  • : FunderStipendienfonds der Basler Chemischen Industrie
  • : Grant ID
  • : Project Title
  • : FunderSwiss National Science Foundation
  • : Grant ID
  • : Project Title
  • : FunderF. Hoffmann-La Roche AG, Basel
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  • : Project Title

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