Structural insight into hybrid peptide ε-helices

Misra, Rajkumar; George, Gijo; Reja, Rahi M.; Dey, Sanjit; Raghothama, Srinivasarao; Gopi, Hosahudya N.

doi:10.1039/c9cc07413a

Cited by 5 publications

(9 citation statements)

References 32 publications

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“…Peptides/fragments were purified using column chromatography and the final purification was done using Preparative HPLC. Purified peptides were characterized using analytical HPLC (Figures S10-S15), ESI-MS (Figures S16-S21), 1 H (Figures S22-S27) and 13 C NMR (Figures S28-33).…”

Section: Resultsmentioning

confidence: 99%

“…(m, 1H), 2.50-2.24 (m, 3H), 2.04 (s, 3H), 1.44 (s, 12H), 1.28 (s, 9H). 13 C {1H} NMR (150 MHz, Chloroform-d) (Figure S9): δ 178.9, 51.9, 34.7, 34.7, 29.4, 28.4, 27.3.…”

Section: Boc-γ 33 -Ohmentioning

confidence: 99%

“…1 H NMR (600 MHz, Chloroform-d) (Figure S22): δ 6.70 (b, 1H), 6.63 (s, 1H), 5.00 (b, 1H), 3.73 (s, 3H), 3.28-3.20 (m, 2H), 1.75-1.71 (m, 2H), 1.54 (s, 6H), 1.47 (s, 6H), 1.44 (s, 9H), 1.19 (s, 6H). 13 C {1H} NMR (150 MHz, Chloroform-d) (Figure S28): δ 176.7, 175.2, 174.9, 154.7, 56.6, 56.3, 52.5, 41.2, 39.3, 36.5, 28.3, 25.9, 24.9. H NMR (600 MHz, Chloroform-d) (Figure S23): δ 7.47 (s, 1H), 6.99 (s, 1H), 4.96 (s, 1H), 3.71 (s, 3H), 3.20 (d, J = 6.7 Hz, 2H), 2.04 (s, 2H), 1.53 (s, 6H), 1.50 (s, 6H), 1.44 (s, 9H), 0.99 (s, 6H).…”

Section: Characterization Of Peptidesboc-aib-γ 22 -Aib-ome (P1-tri)mentioning

confidence: 99%

“…H NMR (600 MHz, Chloroform-d) (Figure S23): δ 7.47 (s, 1H), 6.99 (s, 1H), 4.96 (s, 1H), 3.71 (s, 3H), 3.20 (d, J = 6.7 Hz, 2H), 2.04 (s, 2H), 1.53 (s, 6H), 1.50 (s, 6H), 1.44 (s, 9H), 0.99 (s, 6H). 13 H NMR (600 MHz, Chloroform-d) (Figure S24): δ 6.52 (b, 1H), 6.43 (s, 1H), 4.98 (s, 1H), 3.72 (s, 3H), 2.21-2.14 (m, 2H), 2.06 (dd, J = 9.2, 6.3 Hz, 2H), 1.51 (s, 6H), 1.46 (s, 6H), 1.45 (s, 9H), 1.29 (s, 6H). 13 C {1H} NMR (150 MHz, Chloroform-d) (Figure S30): δ 173.98, 173.10, 77.24, 57.0, 56.1, 53.2, 52.5, 35.3, 31.6, 28.3, 27.0, 24.9.…”

Section: Characterization Of Peptidesboc-aib-γ 22 -Aib-ome (P1-tri)mentioning

confidence: 99%

“…1 H NMR (600 MHz, Chloroform-d) (Figure S4): δ 6.41 (t, J = 6.0 Hz, 1H), 4.68 (b, 1H), 3.17 (b, J = 6.6 Hz, 3H), 1.78 (q, J = 7.8, 6.6 Hz, 3H), 1.51-1.40 (m, 15H), 1.48 (s, 6H), 1.27-1.19 (m, 10H). 13 C {1H} NMR (150 MHz, Chloroform-d) (Figure S7): δ 183.0, 155.9, 79.3, 40.9, 40.4, 39.9, 38.1, 37.1, 28.4, 25.1, 24.9.…”

Section: Purificationmentioning

confidence: 99%

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Helices in Peptides Containing Differentially Geminally Di‐substituted γ Amino Acid Residues

2023

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We have explored the relative propensity of the three differentially di-substituted γ amino acid residues, to be accommodated in all α helical conformations. We have established that small chiral hybrid peptides Boc-Aib-γ x,x -Aib-Leu-Aib-Val-OMe (x,x = 2,2/3,3/4,4) containing single geminally di-substituted γ amino acid residue, can adopt both handedness of helical conformation in crystals and solution. The relative ease of being accommodated in helical structures decreased in the order γ 4,4 > γ 3,3 > γ 2,2 . γ 4,4 and γ 3,3 readily adopted C 12 helical conformations unlike γ 2,2 . γ 2,2 and γ 3,3 containing peptides, adopted either handedness of the helical conformation in crystals while in solution, they adopted right-handed helical conformation. Peptide, containing γ 4,4 only adopted righthanded helical conformation both in the solid and solution states. Our studies established that position of di-substitution along the backbone of γ amino acid residues determined their conformational preference, and thus might be used to generate diversity in the peptide conformations.

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Section: Resultsmentioning

confidence: 99%

“…(m, 1H), 2.50-2.24 (m, 3H), 2.04 (s, 3H), 1.44 (s, 12H), 1.28 (s, 9H). 13 C {1H} NMR (150 MHz, Chloroform-d) (Figure S9): δ 178.9, 51.9, 34.7, 34.7, 29.4, 28.4, 27.3.…”

Section: Boc-γ 33 -Ohmentioning

confidence: 99%

Section: Characterization Of Peptidesboc-aib-γ 22 -Aib-ome (P1-tri)mentioning

confidence: 99%

Section: Characterization Of Peptidesboc-aib-γ 22 -Aib-ome (P1-tri)mentioning

confidence: 99%

Section: Purificationmentioning

confidence: 99%

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Helices in Peptides Containing Differentially Geminally Di‐substituted γ Amino Acid Residues

2023

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Effect of Differential Backbone Di‐substitution of Gamma Amino Acid Residues on the Conformation and Assembly of their Fmoc Derivatives in Solid and Solution States

Debnath

Ghosh

Vasudev

et al. 2022

Chemistry An Asian Journal

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We studied the effect of variable backbone dimethyl-substitution of γ amino acid residues (γ 2,2 , γ 3,3 and γ 4,4 ) on the conformation and assembly, in crystals and solution of their Fmoc derivatives. The crystal structure of γ 2,2 and γ 4,4 derivatives showed distinct conformations (open/close for γ 2,2 /γ 4,4 ) that differed in torsion angles, hydrogen-bonding and most importantly the π-π Fmoc-stacking interactions (relatively favourable for γ 4,4 -close). Fmoc derivatives existed in an equilibrium between major-monomeric (low energy, non-hydrogen bonded) and minor-dimeric (high energy, hydrogen bonded) populations in solution. The rate of major/ minor population exchange was dependent on the position of substitution, highest being for γ 4,4 derivative. In solution, assembly of Fmoc derivatives was solvent dependent, but it was independent of the position of geminal substitution. Crystallization was primarily governed by the stabilization of high-energy dimer by favourable π-π stacking involving Fmoc moieties. High free-energy of the dimers (γ 2,2 -close, γ 3,3open/close) offset favourable stacking interactions and hindered crystallization.

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Microwave-assisted synthesis of peptidomimetic trans-delta-aminopent-3-enoic acid and its derivatives

Saranraj,

Raja

2024

New J. Chem.

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Structural insight into hybrid peptide ε-helices

Abstract: Unique ε-helical organizations (11-helices) from β,γ-hybrid peptides composed of chiral β3-amino acids along with achiral 3,3- or 4,4-dimethyl substituted γ-amino acids are disclosed.

Cited by 5 publications

References 32 publications

Helices in Peptides Containing Differentially Geminally Di‐substituted γ Amino Acid Residues

Helices in Peptides Containing Differentially Geminally Di‐substituted γ Amino Acid Residues

Effect of Differential Backbone Di‐substitution of Gamma Amino Acid Residues on the Conformation and Assembly of their Fmoc Derivatives in Solid and Solution States

Microwave-assisted synthesis of peptidomimetic trans-delta-aminopent-3-enoic acid and its derivatives

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