Impact of α,β-dehydroamino acid residues on the binding abilities of di-, tri- and tetra-peptides

Świa̧tek-Kozłowska, Jolanta; Brasuń, Justyna; Chruściński, Longin; Chruscinska, Elzbieta; Makowski, Maciej; Kozłowski, Henryk

doi:10.1039/b004790m

Cited by 15 publications

(22 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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

View full text Add to dashboard Cite

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.

show abstract

“…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

View full text Add to dashboard Cite

show abstract

“…The coordination pattern for the Cu(II) complexes with the discussed above pentapeptides is the same as that found earlier for parent and mono-substituted shorter peptides [4,5]. The coordination of metal ion starts at the N-terminal amino group and with increasing pH successive deprotonated amide nitrogens are involved.…”

Section: Discussionmentioning

confidence: 60%

“…The binding mode for this complex is {N À , N À , N À , N À }, probably. The low log K Ã values for the species 2N, 3N and 4N ( Table 4) clearly indicate that in studied here ligands the metal ion binding to amide nitrogens is much easier than in the parent peptides [4,5].…”

Section: Discussionmentioning

confidence: 86%

See 1 more Smart Citation

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

Brasuń

Makowski

Ołdziej

et al. 2004

Journal of Inorganic Biochemistry

Self Cite

View full text Add to dashboard Cite

“…Kozlowska and co-workers [8] observed that insertion of a dehydroamino acid residue into di-, tri-or tetrapeptide sequences has considerably changed the binding abilities of these peptide ligands towards metal ions. Alternariolide (AM-toxin) is a cyclic tetradepsipeptide containing a dehydroalanine residue as one of the unusual amino acid and found to be responsible for the necrotic brown spots on certain apple leaves.…”

Section: Modification Of Peptides By Formationmentioning

confidence: 98%

Post-assembly Peptide Modifications by Chemical Methods

Kotha¹,

Lahiri

2005

CMC

View full text Add to dashboard Cite

The demand for peptide drugs is increasing and in this context, "post-assembly (or post-translational) peptide modification strategies" by chemical manipulation of intact oligo-peptides has provided several analogues. Compounds prepared by this method are useful therapeutic molecules for structure activity studies. Herein, we describe various chemical methods such as cross-coupling reactions, cycloaddition reactions, radical reactions and ring-closing metathesis reactions that are useful for post-translational peptide modifications.

show abstract

Impact of α,β-dehydroamino acid residues on the binding abilities of di-, tri- and tetra-peptides

Cited by 15 publications

References 6 publications

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

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

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

Post-assembly Peptide Modifications by Chemical Methods

Contact Info

Product

Resources

About