Coordination ability of pentapeptides with two dehydro-amino acid residues inserted into their sequences

Brasuń, Justyna; Makowski, Maciej; Ołdziej, Stanisław; Świa̧tek-Kozłowska, Jolanta

doi:10.1016/j.jinorgbio.2004.04.014

Cited by 10 publications

(13 citation statements)

References 17 publications

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“…The synthesis of the title compound was described by Brasuń et al (2004). The crystals were grown by slow diffusion of hexane into an ethyl acetate-methanol (20:1 v/v) solution of the compound at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…Dehydropeptides [peptides containing dehydroamino acid residue(s) in their sequences] show enhanced resistance to enzymatic degradation (Shimohigashi et al, 1987). The insertion of dehydroamino acid residues into the peptide sequence also results in a distinct increase of the binding ability of dehydropeptides to metal ions (Brasuń et al, 2004). The dehydroamino acid residues restrict the conformation of the peptide backbone in dehydropeptides and they are strong inducers of folded conformations (Singh & Kaur, 1996).…”

Section: Commentmentioning

confidence: 99%

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N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanyl]glycine methyl ester dihydrate

et al. 2006

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The title pentapeptide, Boc0—Gly1–ΔZPhe2—Gly3–ΔEPhe4—Gly5—OMe, C30H35N5O8·2H2O, adopts the type I β‐turn conformation for the ΔZPhe2—Gly3 residues. It is stabilized by a intramolecular hydrogen bond between the ΔEPhe4 NH and Gly1 CO groups. All the amino acid residues in the pentapeptide sequence are linked trans to each other. The crystal structure is stabilized by intra‐ and intermolecular hydrogen bonds.

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Section: Methodsmentioning

confidence: 99%

Section: Commentmentioning

confidence: 99%

N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanyl]glycine methyl ester dihydrate

et al. 2006

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“…Their presence in peptides results in the enhanced resistance to enzymatic degradation 11. Dehydropeptides also show increased binding ability to metal ions 12, 13…”

Section: Introductionmentioning

confidence: 99%

Combined effect of the ΔPhe or ΔAla residue and the p‐nitroanilide group on a didehydropeptides conformation

et al. 2007

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Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA.TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = Delta(Z)Phe and DeltaAla, were studied with NMR in DMSO and CDCl(3)-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the DeltaPhe residue next to Phe are folded whereas peptides with Gly between DeltaPhe and Phe are less ordered. NMR spectra of DeltaAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual position of the dehydroamino acid residue and the p-NA group. They indicate that all dehydropeptides with the DeltaPhe residue, Boc-Gly-DeltaAla-Phe-p-NA, and Boc-Gly-Gly-DeltaAla-Phe-p-NA adopt ordered conformations in all solvents studied, presumably of the beta-turn type. The last two peptides exhibit surprising chiroptical properties. Their spectra show exciton coupling-like couplets in the region of the p-NA group absorption. This shape of CD spectra suggests a rigid, chiral conformation with a fixed disposition of the p-NA group. The CD spectra indicate that Boc-Gly-DeltaAla-Gly-Phe-p-NA and Gly-DeltaAla-Gly-Phe-p-NA.TFA are unordered, independently of the solvent.

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“…This phenomenon has been explained by the unique amide nitrogen of the dehydroamino acid. 11,12 Even at a relatively low pH, metal ions such as Zn II and Co II are capable of forming strong complex species with the dehydroamino acid s enamide nitrogen. 12 Brasun and coworkers also found that the side chain steric bulk and the E/Z-isomeric form of the dehydroamino acid greatly impact its ability to bind certain Cu II species.…”

Section: Biophysical Properties Of Dehydroamino Acids and Dehydroamino Acid Peptidesmentioning

confidence: 99%

Solid-Phase Total Synthesis of Dehydrotryptophan-Bearing Cyclic Peptides Tunicyclin B, Sclerotide A, CDA3a, and CDA4a using a Protected β-Hydroxytryptophan Building Block

2021

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Coordination ability of pentapeptides with two dehydro-amino acid residues inserted into their sequences

Cited by 10 publications

References 17 publications

N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanyl]glycine methyl ester dihydrate

N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanyl]glycine methyl ester dihydrate

Combined effect of the ΔPhe or ΔAla residue and the p‐nitroanilide group on a didehydropeptides conformation

Solid-Phase Total Synthesis of Dehydrotryptophan-Bearing Cyclic Peptides Tunicyclin B, Sclerotide A, CDA3a, and CDA4a using a Protected β-Hydroxytryptophan Building Block

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