Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Jewgiński, Michał; Krzciuk-Gula, Joanna; Makowski, Maciej; Latajka, Rafał; Kafarski, Paweł

doi:10.3762/bjoc.10.58

Cited by 8 publications

(4 citation statements)

References 46 publications

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“…The three most widely examined conformational preferences are those of ΔAla‐containing, ΔLeu‐containing, and ΔPhe‐containing peptides. In particular, the published computational and experimental 3D structural analyses provide clear evidence that the fully extended (C 5 ) conformation is that largely preferred by ΔAla homo‐peptides to the octamer level . Multiple consecutive C 5 structures, which generate the 2.0 5 ‐helix , predominate in solvents of low polarity and occur in the crystal state.…”

Section: Cαβ‐didehydro‐α‐amino Acid‐containing Peptidesmentioning

confidence: 99%

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Handedness preference and switching of peptide helices. Part II: Helices based on noncodedα‐amino acids

Crisma¹,

Zotti

Formaggio

et al. 2015

Journal of Peptide Science

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In this second part of our review article on the preferred screw sense and interconversion of peptide helices, we discuss the most significant computational and experimental data published on helices formed by the most extensively investigated categories of noncoded α-amino acids. They are as follows: (i) N-alkylated Gly residues (peptoids), (ii) C(α) -alkylated α-amino acids, (iii) C(α,β) -sp(2) configurated α-amino acids, and (iv) combinations of residues of types (ii) and (iii). With confidence, the large body of interesting papers examined and classified in this editorial effort will stimulate the development of helical peptides in many diverse areas of biosciences and nanosciences.

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Section: Cαβ‐didehydro‐α‐amino Acid‐containing Peptidesmentioning

confidence: 99%

“…Privileged solution conformations of Δ Z Phe‐based peptides were satisfactorily determined by NMR analysis . Short peptides containing Δ Z Phe residues were generally shown to fold into conformations that may be perturbed by the H‐bonding capabilities of the solvent.…”

Section: Cαβ‐didehydro‐α‐amino Acid‐containing Peptidesmentioning

confidence: 99%

Handedness preference and switching of peptide helices. Part II: Helices based on noncodedα‐amino acids

Crisma¹,

Zotti

Formaggio

et al. 2015

Journal of Peptide Science

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“…Dehydroamino acids continuously attract attention in various areas, mainly in synthesis, as designed products or suitable substrates, including asymmetric hydrogenation as well as in the conformational studies . Dehydrophenylalanine (ΔPhe), although scarcely presented in natural compounds, is the most often studied dehydroamino acid . This is mainly due to its relatively high stability as well as promising works on dehydrophenylalanyl analogs of naturally occurred peptides .…”

Section: Introductionmentioning

confidence: 99%

Conformational preferences and synthesis of isomers Z and E of oxazole‐dehydrophenylalanine

et al. 2016

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Dehydrophenylalanine, ΔPhe, is the most commonly studied α,β-dehydroamino acid. In nature, further modifications of the α,β-dehydroamino acids were found, for example, replacement of the C-terminal amide group by oxazole ring. The conformational properties of oxazole-dehydrophenylalanine residue (ΔPhe-Ozl), both isomers Z and E, were investigated. To determine all possible conformations, theoretical calculations were performed using Ac-(Z/E)-ΔPhe-Ozl(4-Me) model compounds at M06-2X/6-31++G(d,p) level of theory. Ac-(Z/E)-ΔPhe-Ozl-4-COOEt compounds were synthesized and the conformational preferences of each isomer, Z and E, were investigated using FTIR and NMR-NOE in solutions of increasing polarity (CHCl3 , DMSO-d6). The solid-state low-temperature structures of Ac-(Z)-ΔPhe-Ozl-4-COOEt and its intermediate analog Ac-(Z)-ΔPhe-Ozn(4-OH)-4-COOEt were also determined. In a weakly polar environment, the ΔPhe-Ozl residue has a tendency to adopt the conformation β2 with the calculated φ and ψ angles of -127° and 0° for the isomer Z and -170° and 26° for the isomer E. The increase of environment polarity favors the helical conformation α and the beta-turn like conformation β, but the conformation β2 seems to be still accessible. The (E)-ΔPhe-Ozl residue can be obtained from the isomer Z in photoisomerization reaction. However, hydroxyl-oxazoline-dehydrophenylalanine ΔPhe-Ozn(4-OH) decomposes in such conditions. Alternatively, (E)-ΔPhe-NH2 can be applied as a substrate in the Hantzsch reaction. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 283-294, 2016.

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“…8,9 Dehydropeptides might be also considered as a class of promising foldamers 10 because of their ability to take specific three-dimensional structure forms resulting from the presence of a double bond between the Cα and Cβ atoms, which causes the coupling of this double bond with flanking amide fragments and results in rigid structure of the peptide chain. [11][12][13][14] Numerous studies dealing with dehydropeptide structure and conformation have used Z ΔPhe containig peptides owing to their easy chemical synthesis and substantial stability upon storage, [15][16][17][18] whereas peptides containing E ΔPhe are scarcely described in the literature. This is because E-dehydroamino acids and their peptides are unstable and slowly undergo thermal isomerization upon conditions of peptide synthesis.…”

Section: Introductionmentioning

confidence: 99%

Kinetics of photochemical isomerization of TFA-Gly-ZΔPhe into TFA-Gly-EΔPhe

Makowski¹,

Jewgiński²,

Hurek³

et al. 2017

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The kinetics of photoisomerization of trifluoroacetyl-(Z)-dehydrophenylalanylglycine into trifluoroacetyl-(E)-dehydrophenylalanylglycine was studied in the hope that light-induced reaction could be useful as a means of preparation of the E-dehydropeptides. The obtained results indicate that if this reaction carried out under irradiation with light of wavelength 360 nm it is practically irreversible and gave nearly quantitatively pure Eisomer Significantly, expected cyclic side-products were not observed in the reaction mixture, thus proving the preparative potential of the elaborated procedure.

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Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Cited by 8 publications

References 46 publications

Handedness preference and switching of peptide helices. Part II: Helices based on noncodedα‐amino acids

Handedness preference and switching of peptide helices. Part II: Helices based on noncodedα‐amino acids

Conformational preferences and synthesis of isomers Z and E of oxazole‐dehydrophenylalanine

Kinetics of photochemical isomerization of TFA-Gly-ZΔPhe into TFA-Gly-EΔPhe

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