<i>N</i>-Aminoazetidinecarboxylic Acid: Direct Access to a Small-Ring Hydrazino Acid

Declerck, Valérie; Aitken, David J.

doi:10.1021/jo102108t

Cited by 26 publications

(20 citation statements)

References 42 publications

(24 reference statements)

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“…Organicsyntheses General remarks:C ompounds (+)-Boc-(trans-ACBC)-OH, (+ +)-Boc-(cis-ACBC)-OH and (+)-Boc-AAzC-OH were prepared according to literature procedures. [63,64] All reagents and solvents were of commercial grade and were used without further purification. Dichloromethane was dried over activated alumina.…”

Section: Methodsmentioning

confidence: 99%

Intrinsic Folding Proclivities in Cyclic β‐Peptide Building Blocks: Configuration and Heteroatom Effects Analyzed by Conformer‐Selective Spectroscopy and Quantum Chemistry

Alauddin

Gloaguen

Brenner

et al. 2015

Chemistry A European J

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This work describes the use of conformer-selective laser spectroscopy following supersonic expansion to probe the local folding proclivities of four-membered ring cyclic β-amino acid building blocks. Emphasis is placed on stereochemical effects as well as on the structural changes induced by the replacement of a carbon atom of the cycle by a nitrogen atom. The amide A IR spectra are obtained and interpreted with the help of quantum chemistry structure calculations. Results provide evidence that the building block with a trans-substituted cyclobutane ring has a predilection to form strong C8 hydrogen bonds. Nitrogen-atom substitution in the ring induces the formation of the hydrazino turn, with a related but distinct hydrogen-bonding network: the structure is best viewed as a bifurcated C8/C5 bond with the N heteroatom lone electron pair playing a significant acceptor role, which supports recent observations on the hydrazino turn structure in solution. Surprisingly, this study shows that the cis-substituted cyclobutane ring derivative also gives rise predominantly to a C8 hydrogen bond, although weaker than in the two former cases, a feature that is not often encountered for this building block.

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Section: Methodsmentioning

confidence: 99%

Intrinsic Folding Proclivities in Cyclic β‐Peptide Building Blocks: Configuration and Heteroatom Effects Analyzed by Conformer‐Selective Spectroscopy and Quantum Chemistry

Alauddin

Gloaguen

Brenner

et al. 2015

Chemistry A European J

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“…17). 40 Utilizing conditions developed by the Swenton group, azetidine 54 was accessed by irradiating 6-azauracil (53) and ethylene with UV light in the presence of acetone as a photosensitizer. A subsequent synthetic sequence involving Boc-protection, hydrolysis, chiral resolution and deprotection afforded 58 in high yield.…”

Section: Synthetic Applicationsmentioning

confidence: 99%

Synthesis of azetidines by aza Paternò–Büchi reactions

2020

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“…[17,18] The1 2-helix preference of tACBC oligomers raises the question of the sustainability of an 8-helix ( Figure 1); indeed, in previous cases where 12-helix conformers compete, the 8-helix was only observed for small ( 4-mer) oligomers. [17] N-Aminoazetidine-2-carboxylic acid (AAzC) [19] is an aza analogue of tACBC and is characterized by as trong tendency to form ab ifurcated C8/5-ring H-bonded structure known as ahydrazino (Hz) turn ( Figure 1). [20,21] We therefore examined the ability of asingle AAzC residue to behave as an "8-helix primer" when employed as the N-terminal residue in an oligo-tACBC sequence.…”

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confidence: 99%

Fine Tuning of β‐Peptide Foldamers: a Single Atom Replacement Holds Back the Switch from an 8‐Helix to a 12‐Helix

et al. 2015

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Cyclic homologated amino acids are important building blocks for the construction of helical foldamers. N-aminoazetidine-2-carboxylic acid (AAzC), an aza analogue of trans-2-aminocyclobutanecarboxylic acid (tACBC), displays a strong hydrazino turn conformational feature, which is proposed to act as an 8-helix primer. tACBC oligomers bearing a single N-terminal AAzC residue were studied to evaluate the ability of AAzC to induce and support an 8-helix along the oligopeptide length. While tACBC homooligomers assume a dominant 12-helix conformation, the aza-primed oligomers preferentially adopt a stabilized 8-helix conformation for an oligomer length up to 6 residues. The (formal) single-atom exchange at the N terminus of a tACBC oligomer thus contributes to the sustainability of the 8-helix, which resists the switch to a 12-helix. This effect illustrates atomic-level programmable design for fine tuning of peptide foldamer architectures.

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N-Aminoazetidinecarboxylic Acid: Direct Access to a Small-Ring Hydrazino Acid

Cited by 26 publications

References 42 publications

Intrinsic Folding Proclivities in Cyclic β‐Peptide Building Blocks: Configuration and Heteroatom Effects Analyzed by Conformer‐Selective Spectroscopy and Quantum Chemistry

Intrinsic Folding Proclivities in Cyclic β‐Peptide Building Blocks: Configuration and Heteroatom Effects Analyzed by Conformer‐Selective Spectroscopy and Quantum Chemistry

Synthesis of azetidines by aza Paternò–Büchi reactions

Fine Tuning of β‐Peptide Foldamers: a Single Atom Replacement Holds Back the Switch from an 8‐Helix to a 12‐Helix

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