Non‐classical Helices with <i>cis</i> Carbon–Carbon Double Bonds in the Backbone: Structural Features of α,γ‐Hybrid Peptide Foldamers

Kumar, Mothukuri Ganesh; Thombare, Varsha J.; Katariya, Mona M.; Veeresh, Kuruva; Kalpana, R.; Gopi, Hosahudya N.

doi:10.1002/ange.201602861

Cited by 4 publications

(1 citation statement)

References 77 publications

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“…We have been interested in understanding the conformations and self‐assembly of hybrid peptides containing 1 : 1 alternating α‐ and γ‐amino acids [24d,g] . Previously, we reported peptide nanotubes derived from the α,γ‐hybrid peptide 12‐helix and their utility in casting the silver nanowire from silver ions [27] . In continuation, we sought to investigate the conformations of α,γ‐hybrid peptides containing Cys residues, which can dimerize the hybrid peptide foldamers and also provide a useful handle to conjugate different functional groups on the surface of the self‐assembled foldamers architectures.…”

Section: Introductionmentioning

confidence: 99%

Foldamer Nanotubes Mediated Label‐Free Detection of Protein‐Small Molecule Interactions

Kumar

Bhat

Dey

et al. 2023

Chemistry A European J

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Development of miniaturized lab‐on‐chip devices for the detection of rapid and specific small molecule‐protein binding interactions at very low concentrations holds significant importance in drug discovery and biomedical applications. Here, the label‐free detection of small molecule‐protein interactions is reported on the surface functionalizable nanotubes of α,γ‐hybrid peptide helical foldamers using nanoscale capacitance and impedance spectroscopy. The 12‐helix conformation of the α,γ‐hybrid peptide observed in the single crystals, self‐assembled into nanotubes in an aqueous environment with exposed cysteine thiols for small molecule conjugation. The binding of streptavidin to the covalently linked biotin on the surface of nanotubes was detected at the picomolar concentrations. No change in the capacitance and impedance were observed in the absence of either immobilized biotin or protein streptavidin. The functionalizable hybrid peptide nanotubes reported here pave the way for the label‐free detection of various small molecule protein interactions at very low concentrations.

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Section: Introductionmentioning

confidence: 99%

Foldamer Nanotubes Mediated Label‐Free Detection of Protein‐Small Molecule Interactions

Kumar

Bhat

Dey

et al. 2023

Chemistry A European J

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View full text Add to dashboard Cite

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Artificial β‐Double Helices from Achiral γ‐Peptides

et al. 2017

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Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d‐peptides. In contrast to natural polypeptides, remarkable β‐double‐helical structures from achiral γ‐peptides built from α,β‐unsaturated γ‐amino acids have been observed. The crystal structures suggest that they adopted parallel β‐double helical structures and these structures are stabilized by the interstrand backbone amide H‐bonds. Furthermore, both NMR spectroscopy and fluorescence studies support the existence of double‐helical conformations in solution. Although a variety of folded architectures featuring distinct H‐bonds have been discovered from the β‐ and γ‐peptide foldamers, this is the first report to show that achiral γ‐peptides can spontaneously intertwine into β‐double helical structures.

show abstract

Artificial β‐Double Helices from Achiral γ‐Peptides

et al. 2017

Self Cite

View full text Add to dashboard Cite

Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d-peptides. In contrast to natural polypeptides, remarkable β-double-helical structures from achiral γ-peptides built from α,β-unsaturated γ-amino acids have been observed. The crystal structures suggest that they adopted parallel β-double helical structures and these structures are stabilized by the interstrand backbone amide H-bonds. Furthermore, both NMR spectroscopy and fluorescence studies support the existence of double-helical conformations in solution. Although a variety of folded architectures featuring distinct H-bonds have been discovered from the β- and γ-peptide foldamers, this is the first report to show that achiral γ-peptides can spontaneously intertwine into β-double helical structures.

show abstract

Non‐classical Helices with cis Carbon–Carbon Double Bonds in the Backbone: Structural Features of α,γ‐Hybrid Peptide Foldamers

Cited by 4 publications

References 77 publications

Foldamer Nanotubes Mediated Label‐Free Detection of Protein‐Small Molecule Interactions

Foldamer Nanotubes Mediated Label‐Free Detection of Protein‐Small Molecule Interactions

Artificial β‐Double Helices from Achiral γ‐Peptides

Artificial β‐Double Helices from Achiral γ‐Peptides

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