Molecular Architecture with Functionalized β‐Peptide Helices

Brückner, Arndt M.; Chakraborty, Pradip; Gellman, Samuel H.; Diederichsen, Ulf

doi:10.1002/anie.200351871

Cited by 70 publications

(52 citation statements)

References 30 publications

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“…[11] Figure 3. Temperature-dependent UV spectra of self-aggregating oligomers 13 (T Z GAT) and 14 (TGAT).…”

Section: Resultsmentioning

confidence: 98%

“…[10] Recently, we reported on nucleobase-functionalized β-peptide 14-helices and their reversible, antiparallel, and selective organization by nucleobase recognition (Figure 1). [11] Base-pairing provides an excellent driving force and selectivity for the organization of β-peptide helices similar to that in the known self-association of unnatural oligomers like peptidic nucleic acids [12,13] and α-helical peptides. [14] In the series of nucleobase-modified β-peptides the high helical content leads to a preorganization of the attached nucleobases with respect to double-strand formation.…”

Section: Introductionmentioning

confidence: 99%

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Synthesis of a 7‐Deazaguanine‐Functionalized β‐Amino Acid: Improved Specificity of β‐Peptide Helix Organization

2006

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Nucleobase‐functionalized β‐peptides are a suitable scaffold for the construction of well‐defined tertiary structures organized by nucleobase pair recognition. Since guanine‐rich oligomers are especially known to form higher aggregates, an enantiomerically pure 7‐deazaguanine (zG)‐functionalized nucleo‐β3‐amino acid was synthesized from a β‐lactam derivative as a key intermediate. Incorporated into β‐peptide 14‐helices it was possible to reduce aggregation phenomena and to increase recognition selectivity. Evidence for base‐pair‐mediated helix recognition was obtained by temperature‐dependent UV and CD spectroscopy. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006)

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“…[11] Figure 3. Temperature-dependent UV spectra of self-aggregating oligomers 13 (T Z GAT) and 14 (TGAT).…”

Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Synthesis of a 7‐Deazaguanine‐Functionalized β‐Amino Acid: Improved Specificity of β‐Peptide Helix Organization

2006

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“…As opposed to the "binary" α-helix and β-sheet conformations of natural oligopeptides, β-peptides exhibit a range of -mostly helicalsecondary structures [15]. Of particular interest are β 3 -peptides that fold into helices consisting 14-membered loops through hydrogen bonding between C=O of residues i and the N-H of the i-3 residue [16,17]. Accordingly, these so-called 14-helices exhibit a pitch of 3.0-3.1 amino acids per turn that is a substantial advantage over the α-helix that exhibits 3.6 residues per turn [16,18,19].…”

Section: Introductionmentioning

confidence: 99%

“…Of particular interest are β 3 -peptides that fold into helices consisting 14-membered loops through hydrogen bonding between C=O of residues i and the N-H of the i-3 residue [16,17]. Accordingly, these so-called 14-helices exhibit a pitch of 3.0-3.1 amino acids per turn that is a substantial advantage over the α-helix that exhibits 3.6 residues per turn [16,18,19]. In the 14-helix the side chains align along the helix, providing a geometrically determined structure that is an ideal scaffold for a self-assembling building block [18,20].…”

Section: Introductionmentioning

confidence: 99%

Co-assembly of helical β³-peptides: a self-assembled analogue of a statistical copolymer

Buchanan

Garvey

Perlmutter

et al. 2017

Pure and Applied Chemistry

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Unnatural peptide self-assembly offers the means to design hierarchical nanostructures of controlled geometries, chemical function and physical properties. N-acyl β 3 peptides, where all residues are unnatural amino acids, are able to form helical fibrous structures by a head-to-tail assembly of helical monomers, extending the helix via a three point supramolecular hydrogen bonding motif. These helical nanorods were shown to be stable under a wide range of physical conditions, offering a self-assembled analogue of polymeric fibres. Hitherto the self-assembly has only been demonstrated between identical monomers; however the self-assembly motif is sequence-independent, offering the possibility of hetero-assembly of different peptide monomers. Here we present a proof of principle study of head-to-tail co-assembly of two different helical unnatural peptides Ac-β [LIA], where the letters denote the β 3 analogues of natural amino acids. By atomic force microscopy imaging it was demonstrated that the homo-assembly and co-assembly of these peptides yield characteristically different structures. Synchrotron small angle X-ray scattering experiments have confirmed the presence of the fibres in the solution and the averaged diameters from modelled data correlate well to the results of AFM imaging. Hence, there is evidence of co-assembly of the fibrous superstructures; given that different monomers may be used to introduce variations into chemical and physical properties, the results demonstrate a self-assembled analogue of a statistical co-polymer that can be used in designing complex functional nanomaterials.

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“…123 A helix dimer formation through complexation of the zinc ion was carried out by the incorporation of zinc-binding motifs in the β-peptide sequence. 124 Crystal engineering has been elegantly applied for the molecular architecture of helices.…”

Section: Higher-ordered Helical Motifsmentioning

confidence: 99%

β-Peptide foldamer helices with tailored diameters

Szolnoki¹

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Molecular Architecture with Functionalized β‐Peptide Helices

Cited by 70 publications

References 30 publications

Synthesis of a 7‐Deazaguanine‐Functionalized β‐Amino Acid: Improved Specificity of β‐Peptide Helix Organization

Synthesis of a 7‐Deazaguanine‐Functionalized β‐Amino Acid: Improved Specificity of β‐Peptide Helix Organization

Co-assembly of helical β³-peptides: a self-assembled analogue of a statistical copolymer

β-Peptide foldamer helices with tailored diameters

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Molecular Architecture with Functionalized β‐Peptide Helices

Cited by 70 publications

References 30 publications

Synthesis of a 7‐Deazaguanine‐Functionalized β‐Amino Acid: Improved Specificity of β‐Peptide Helix Organization

Synthesis of a 7‐Deazaguanine‐Functionalized β‐Amino Acid: Improved Specificity of β‐Peptide Helix Organization

Co-assembly of helical β3-peptides: a self-assembled analogue of a statistical copolymer

β-Peptide foldamer helices with tailored diameters

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Product

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Co-assembly of helical β³-peptides: a self-assembled analogue of a statistical copolymer