Überraschend stabile helicale Strukturen in α‐β‐Peptiden durch Einbau von <i>cis</i>‐β‐Aminocyclopropancarbonsäuren

Pol, Silvia De; Zorn, Chiara; Klein, Christian; Zerbe, Oliver; Reiser, Oliver

doi:10.1002/ange.200352267

Cited by 60 publications

(15 citation statements)

References 32 publications

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“…For (R/S)-oligoureas 10-13, noticeable chemical shift differ-ences (0.57 < DdA C H T U N G T R E N N U N G ( a CH) < 1.32 ppm) were observed between the diastereotopic a CH protons of the acyclic motifs. Moreover 3 6 ]DMSO were typical of a random configuration, that is, 3 J av = 7.5 AE 0.1 Hz for the S/S series (Tables S11 and S12, and Figure S13 B, the Supporting Information). Numerous crosspeaks were observed on the 2D 1 H ROESY spectra (Tables S14-18, the Supporting Information).…”

Section: Nmr Analysismentioning

confidence: 99%

“…[1,2] The use of amino acid homologues, commonly derived from natural a-amino acids, allowed the design of various helical systems (i.e., 14-, 12-, 10/12-helix), which are substantially enlarged with homo-and heterochiral constrained cyclic derivatives as well as the combination of a-, b-, and g-amino acids to synthesize a/b, a/g, b/g sequences of a particular folding. [3] Although a broad range of amidebased structures has been described with various combinations, the link between building blocks was not so intensively explored. Among the different possibilities of amino acid derivative connections, the urea linkage presents a particularly interesting bifurcated hydrogen-bond stabilization system.…”

Section: Introductionmentioning

confidence: 99%

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Mixed Oligoureas Based on Constrained Bicyclic and Acyclic β‐Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding

André

Legrand

Moulat

et al. 2013

Chemistry A European J

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The combination of a non-functionalized constrained bicyclo[2.2.2]octane motif along with urea linkages allowed the formation of a highly rigid 2.5(12/14) helical system both in solution and the solid state. In this work, we aimed at developing stable and functionalized systems as promising materials for biological applications in investigating the impact of this constrained motif and its configuration on homo and heterochiral mixed-oligourea helix formation. Di-, tetra-, hexa-, and octa-oligoureas alternating the highly constrained bicyclic motif of (R) or (S) configuration with acyclic (S)-β(3)-amino acid derivatives were constructed. Circular dichroism (CD), NMR experiments, and the X-ray crystal structure of the octamer unequivocally proved that the alternating heterochiral R/S sequences form a stable left-handed 2.5-helix in contrast to the mixed (S/S)-oligoureas, which did not adopt any defined secondary structure. We observed that the (-)-synclinal conformation around the C(α)-C(β) bond of the acyclic residues, although sterically less favorable than the (+)-synclinal conformation, was imposed by the (R)-bicyclic amino carbamoyl (BAC) residue. This highlighted the strong ability of the BAC residue to drive helical folding in heterochiral compounds. The role of the stereochemistry of the BAC unit was assessed and a model was proposed to explain the misfolding of the S/S sequences.

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Section: Nmr Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mixed Oligoureas Based on Constrained Bicyclic and Acyclic β‐Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding

André

Legrand

Moulat

et al. 2013

Chemistry A European J

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“…[4,[8][9][10] From the above studies, it is amply evident that mixed helices invariably resulted from heterodipeptide repeats. However, the a/b-dipeptide repeats reported by Gellman and co-workers [12] showed the coexistence of an 11 helix along with a 14/15 helix, whereas Reiser and coworkers [13] observed a 13 helix in the a/b peptides containing alternate cis-b-amino cyclopropane carboxylic acid and l-Ala residues.…”

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confidence: 94%

9/11 Mixed Helices in α/β Peptides Derived from C‐Linked Carbo‐β‐Amino Acid and L‐Ala Repeats

et al. 2005

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“…The pioneering work of Gellman [9] and Seebach [10] on β-peptides designing oligomers of cyclic or acyclic β-amino acids has shown the power of these chemical tools in a number of biological applications. Besides β-peptides, also alternating α/β-peptides, [11] γ-peptides [12] and δ-peptides [13] have been described, and many other foldamers are rapidly emerging. Here, we report our first results concerning the use of Amp as a γ-amino acid to prepare alternating α/γ-peptides by the solid-phase Fmoc methodology.…”

Section: Introductionmentioning

confidence: 99%

An Improved Synthesis of 3,4‐(Aminomethano)proline and Its Incorporation into Small Oligopeptides

et al. 2006

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Starting from the readily available Garner aldehyde, a new synthesis of diastereomerically and enantiomerically pure 3,4‐(aminomethano)prolinol (2R,1′S,3S,4S)‐17 has been developed using simple and easily scalable transformations. The protected diamino alcohol (2R,1′S,3S,4S)‐17 has been shown to be an appropriate compound for the exchange of protecting groups. Final Jones oxidation furnished the correspondingly protected diamino acids in high yields. The newly synthesized Fmoc/Boc‐protected 3,4‐(aminomethano)proline (Amp) derivatives, which are proline mimics as well as bicyclic γ‐amino acids, depending on the orthogonal protecting group pattern, were employed for solid‐phase peptide synthesis with the Fmoc strategy. Thus, the features of Amp as a γ‐amino acid residue (γ‐Amp) were investigated in the preparation of alternating α/γ‐amino acid sequences. The obtained highly homogeneous products were characterized by circular dichroism spectroscopy. The fact that the dichroic properties of the α/γ‐oligopeptides were independent from the solvent used (water or methanol) suggests the presence of a preferred conformation. These results are encouraging for the development of foldamers based on γ‐Amp units. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006)

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Überraschend stabile helicale Strukturen in α‐β‐Peptiden durch Einbau von cis‐β‐Aminocyclopropancarbonsäuren

Cited by 60 publications

References 32 publications

Mixed Oligoureas Based on Constrained Bicyclic and Acyclic β‐Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding

Mixed Oligoureas Based on Constrained Bicyclic and Acyclic β‐Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding

9/11 Mixed Helices in α/β Peptides Derived from C‐Linked Carbo‐β‐Amino Acid and L‐Ala Repeats

An Improved Synthesis of 3,4‐(Aminomethano)proline and Its Incorporation into Small Oligopeptides

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