Linear oligopeptides: c.d. and n.m.r. study of Dnp-pNA derivatives of Aib-containing tetrapeptides in a β-bend conformation

Pieri, Gianfranco De; Signor, A.; Bonora, Gian Maria; Toniolo, Claudio

doi:10.1016/0141-8130(84)90045-x

Cited by 5 publications

(6 citation statements)

References 29 publications

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“…The similar role can be expected of the p ‐NA group. It has been found that this chromophore is a very useful tool in the conformational analysis of peptides 79–82…”

Section: Resultsmentioning

confidence: 99%

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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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“…The similar role can be expected of the p ‐NA group. It has been found that this chromophore is a very useful tool in the conformational analysis of peptides 79–82…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, the results obtained for 1 – 8 indicate that the p ‐NA group may serve as a useful conformational probe in the CD studies on dehydropeptides. The p ‐NA moiety gives a distinct charge‐transfer band far away from the peptide chromophore absorption which facilitates the CD analysis 79–82…”

Section: Discussionmentioning

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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“…In this chromophoric system the two modified amino acid side chains protrude toward the same direction with respect to the cyclic dipeptide average plane 33, 34. In addition, a variety of detailed exciton‐coupled CD analyses have been performed on systems with four amino acid spacers (forming either a single β‐turn or two consecutive β‐turns) but with a less powerful chromophoric dyad (2,4‐dinitrophenylamine/4‐nitroanilide),35–48 unsuitable for long‐range interaction investigations.…”

Section: Resultsmentioning

confidence: 99%

Turn and helical peptide spacers: Combined distance and angular dependencies in the exciton‐coupled circular dichroism of intramolecularly interacting bis‐porphyrins

et al. 2006

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In a previous study we examined by the exciton-coupled circular dichroic method the distance effect generated by three-rigid-turn and helical-peptide spacers. In this connection porphyrins were confirmed to be excellent reporter chromophores. In the present investigation we have completed this research by expanding the original analysis to the assessment of the combined role of the chromophore distance and orientation with use of the same porphyrin derivatives and additional four analogous spacers of different main-chain lengths. We find that not only the intramolecular separation of the chromophores, but the angular dependence between the directions of their effective transition moments as well, are responsible for the onset and modulation of the intensity of the exciton-coupling phenomenon of the porphyrin Soret band.

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“…In an attempt to investigate the effect of incorporating dehydroamino acid residues and the para‐nitroanilide group on dehydropeptide conformation, Lisowski et al carried out conformational studies on two series of dehydropeptides, containing α,β‐didehydrophenylalanine and ΔAla residues, Boc‐Gly‐ΔPhe‐Phe‐ pNA , Boc‐Gly‐Gly‐ΔPhe‐Phe‐ pNA , Gly‐ΔPhe‐Gly‐Phe‐ pNA .TFA, Boc‐Gly‐ΔPhe‐Gly‐Phe‐ pNA , Boc‐Gly‐ΔAla‐Phe‐ pNA , Boc‐Gly‐Gly‐ΔAla‐Phe‐ pNA , Gly‐ΔAla‐Gly‐Phe‐ pNA .TFA, Boc‐Gly‐ΔAla‐Gly‐Phe‐ pNA (pNA stands for para nitroanilide, and TFA for trifluoroacetic acid) 40. CD analysis was facilitated by the presence of pNA moiety that shows a distinct charge‐transfer band far away from the peptide chromophore absorption 41–44. CD and NMR studies showed ΔF containing peptides to be ordered compared to ΔAla peptides, suggesting the influence of mutual disposition of the dehydroamino acid residue and the pNA on the conformational properties 40…”

Section: Introductionmentioning

confidence: 99%

De novo design of α,β-didehydrophenylalanine containing peptides: From models to applications

Gupta

Chauhan

2010

Biopolymers

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The de novo design of peptides and proteins has emerged as an approach for investigating protein structure and function. The success relies heavily on the ability to design relatively short peptides that can adopt stable secondary structures. To this end, substitution with α,β‐dehydroamino acids, especially α,β‐didehydrophenylalanine (ΔPhe or ΔF) has blossomed in manifold directions, providing a rich diversity of well‐defined structural motifs. Introduction of α,β‐didehydrophenylalanine induces β‐bends in small and 310‐helices in longer peptide sequences. Most favorable conformation of ΔF residues are (ϕ,ψ) ∼(60°, 30°), (−60°, −30°), (−60°, 150°), and (60°, −150°). These features have been exploited in designing helix‐turn‐helix, helical bundle arrangements, and glycine zipper type super secondary structural motifs. The unusual capability of α,β‐didehydrophenylalanine ring to form a variety of multicentered interactions (N‐H…O, C‐H…O, C‐H…π, and N‐H…π) suggests its possible exploitation for future de novo design of supramolecular structures. This work has now been extended to the de novo design of peptides with antibiotic, antifibrillization activity, etc. More recently, self‐assembling properties of small dehydropeptides have been explored. This review focuses primarily on the structural and functional behavior of α,β‐didehydrophenylalanine containing peptides. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 161–173, 2011.

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Linear oligopeptides: c.d. and n.m.r. study of Dnp-pNA derivatives of Aib-containing tetrapeptides in a β-bend conformation

Cited by 5 publications

References 29 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

Turn and helical peptide spacers: Combined distance and angular dependencies in the exciton‐coupled circular dichroism of intramolecularly interacting bis‐porphyrins

De novo design of α,β-didehydrophenylalanine containing peptides: From models to applications

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