Folding Propensity of Cyclohexylether-δ-peptides

Arndt, Hans‐Dieter; Ziemer, Burkhard; Koert, Ulrich

doi:10.1021/ol048861q

Cited by 33 publications

(14 citation statements)

References 25 publications

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“…"Aliphatic" foldamers have saturated carbon chains separating amide or urea groups. Example of this group include the - 27,28 , - 29 and - 30,31 , oligoureas 32 , azapeptides 33,34 , pyrrolinones 35 , -aminoxypeptides 36 and sugar-based peptides 37,38 . The second class makes use of aromatic spacers within the backbone.…”

Section: Framework Selectionmentioning

confidence: 99%

Foldamers as versatile frameworks for the design and evolution of function

et al. 2007

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Foldamers are sequence-specific oligomers akin to peptides, proteins and oligonucleotides that fold into well-defined three-dimensional structures. They offer the chemical biologist a broad pallet of building blocks for the construction of molecules that test and extend our understanding of protein folding and function. Foldamers also provide templates for presenting complex arrays of functional groups in virtually unlimited geometrical patterns, thereby presenting attractive opportunities for the design of molecules that bind in a sequence- and structure-specific manner to oligosaccharides, nucleic acids, membranes and proteins. We summarize recent advances and highlight the future applications and challenges of this rapidly expanding field.

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Section: Framework Selectionmentioning

confidence: 99%

Foldamers as versatile frameworks for the design and evolution of function

et al. 2007

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“…After the successful synthesis of various masked amino alcohols such as aryl/alkyl ethanolamines and aryloxy propanolamines with high enantiopurity, enzymatic hydrolysis methodology was envisaged with Arthrobacter sp . lipase, for the kinetic resolution of racemic 2‐amino cycloalkanols and vicinal‐aminoindanols, due to their vast applications in medicinal chemistry and asymmetric synthesis 68–74 . It was found that Arthrobacter sp .…”

Section: Applicationsmentioning

confidence: 99%

A review on Arthrobacter sp. lipase: A versatile biocatalyst for the kinetic resolution to access enantiomerically pure/enriched compounds

et al. 2021

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Over the last few years, there has been a dramatic increase in the number of reports related to Arthrobacter sp. lipase (ABL:MTCC No. 5125) catalyzed kinetic resolution performed in biphasic media. A strain displaying esterase/lipase activity and designated as ABL was isolated, during the course of a screening program at Indian Institute of Integrative Medicine, Jammu. Considerable research has shown that reactions catalyzed by ABL are more selective than many commercial lipases. Since new applications of this lipase are emerging, there is a great need to provide all the relevant information exclusively. This review article is an attempt to cover all the relevant reports based on isolation, purification, immobilization, and application of ABL in the biopharmaceutical sector.

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“…Cyclohexylether-δ-peptides (6) were predicted to form a secondary structure in solution based on their circular dichroism (CD) spectra, although the detailed structure was not confirmed. 33 Oligomers of L-ornithine with an aromatic ring as a side chain (7) were suggested by their NMR analysis to be a stable zipper-featured structure in solution due to the charge-transfer interaction between the alternately-positioned electron-deficient and electron-rich aromatic side chains on the α-amino group. 34 The backbone length of δ-amino acids (NH-C-C-C-C-CO) is analogous to that of a dipeptide unit of natural α-amino acids (NH-C-CO-NH-C-CO), and thus δ-peptides with a stable secondary structure are potentially effective mimetics of functional α-peptides.…”

Section: Introductionmentioning

confidence: 99%

Design, synthesis, and structural characterization of helix-forming aliphatic homo-δ-peptides based on conformational restriction due to the structural characteristics of cyclopropane

Watanabe

Nagata

Doi

et al. 2021

Preprint

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Considerable effort has been directed toward developing artificial peptide-based oligomers that fold into a specific secondary structure, i.e., peptide foldamers. To date, however, detailed structural analysis of crystals of δ-peptide foldamers consisting of aliphatic δ-amino acids, which have a more extended carbon backbone compared with well-studied β- and γ-amino acids, have not been reported. We rationally designed aliphatic homo-δ-peptide foldamers forming a stable helical structure utilizing a chiral cyclopropane δ-amino acid as a monomer unit whose conformation was tightly restricted by the structural characteristics of cyclopropane depending on its stereochemistry. We stereoselectively synthesized the cyclopropane δ-amino acid monomer and prepared its various homo-oligomers. Structural analysis of the homo-δ-peptides using nuclear magnetic resonance, circular dichroism, and infrared spectroscopy revealed that they form a stable 14-helical structure in solution. Furthermore, the effective conformational regulation of the backbone due to the characteristics of cyclopropane allowed us to achieve X-ray crystallographic analysis of the homo-δ-peptides, showing their common right-handed 14-helical structures. The helical structures were consistent with both those predicted by theoretical calculations and those obtained based on nuclear magnetic resonance spectroscopy in solution. A critical point is that the helical structures of these δ-peptides are theoretically predictable by calculations. To our knowledge, this is the first example of aliphatic homo-δ-peptide foldamers forming a stable helical structure both in solution and in crystal.

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Folding Propensity of Cyclohexylether-δ-peptides

Cited by 33 publications

References 25 publications

Foldamers as versatile frameworks for the design and evolution of function

Foldamers as versatile frameworks for the design and evolution of function

A review on Arthrobacter sp. lipase: A versatile biocatalyst for the kinetic resolution to access enantiomerically pure/enriched compounds

Design, synthesis, and structural characterization of helix-forming aliphatic homo-δ-peptides based on conformational restriction due to the structural characteristics of cyclopropane

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