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

Makowski, Maciej; Lisowski, Marek; Maciąg, Anna; Lis, Tadeusz

doi:10.1107/s1600536806002273

Cited by 12 publications

(18 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The C-C distances (C8 C9 and C19 C20) are very similar to those found in other structures containing two ÁPhe residues (Tuzi et al, 1997;Makowski et al, 2005Makowski et al, , 2006. The C-C distances (C8 C9 and C19 C20) are very similar to those found in other structures containing two ÁPhe residues (Tuzi et al, 1997;Makowski et al, 2005Makowski et al, , 2006.…”

Section: Commentsupporting

confidence: 83%

“…In a very similar peptide, Boc-Ala-ÁPhe-Gly-ÁPhe-Ala-OMe, the same central fragment flanked by two chiral alanine residues adopts a right-handed 3 10 -helical conformation (Ciajolo et al, 1990). The N4-H4Á Á ÁO3 hydrogen bond is similar to the hydrogen bond formed in Boc-Gly-Á Z Phe-Gly-Á E Phe-Gly-OMe dihydrate (Makowski et al, 2006). The deviations from the standard values are not larger than 7 with the exception of !…”

Section: Commentmentioning

confidence: 93%

“…Continuing our studies (Makowski et al, 2005(Makowski et al, , 2006(Makowski et al, , 2007 on dehydropeptides containing the ÁPhe residue, in this paper we present the crystal structure of pentapeptide Boc 0 -Gly 1 -Á Z Phe 2 -Gly 3 -Á Z Phe 4 -Gly 5 -OMe. The peptide contains two dehydrophenylalanyl residues of the Z configuration (their phenyl rings are cis to the N atom), each situated between two flexible glycine residues.…”

Section: Commentmentioning

confidence: 94%

See 2 more Smart Citations

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

et al. 2007

Self Cite

View full text Add to dashboard Cite

In the crystal structure of the pentapeptide Boc0—Gly1–ΔZPhe2—Gly3–ΔZPhe4—Gly5—OMe, C30H35N5O8, the values of torsion angles Φ and Ψ show the presence of two type III′β‐turns, at the ΔZPhe2 and Gly3 residues, and Gly3 and ΔZPhe4 residues. All amino acids in the peptide are linked trans to each other. Two intramolecular N—H⋯O hydrogen bonds, between CO and NH groups, stabilize β‐turns present in the peptide.

show abstract

Section: Commentsupporting

confidence: 83%

Section: Commentmentioning

confidence: 93%

Section: Commentmentioning

confidence: 94%

See 1 more Smart Citation

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

et al. 2007

Self Cite

View full text Add to dashboard Cite

show abstract

“…[9][10][11][12] It has been well established that (Z)-DPhe residue has a strong tendency to stabilize b-turns in short model peptides and 3 10 helical conformations in longer peptides. [15][16][17] In non-polar solvents, the extended conformer C 5 (/, w $ 2179 , 162 ) can be also found. 7,14 According to a few literature data, (E)-DPhe adopts in its crystal state the b (/, w $ 242 , 124 ) conformation, or the helical a L (/, w $51 , 49 ) one.…”

Section: Introductionmentioning

confidence: 93%

Toward engineering efficient peptidomimetics. Screening conformational landscape of two modified dehydroaminoacids

et al. 2013

Self Cite

View full text Add to dashboard Cite

Effective peptidomimetics should posses structural rigidity and appropriate interaction pattern leading to potential spatial and electronic matching to the target receptor site. Rational design of such small bioactive molecules could push chemical synthesis and molecular modeling toward faster progress in medicinal chemistry. Conformational properties of N-t-butoxycarbonyl-glycine-(E/Z)-dehydrophenylalanine N',N'-dimethylamides (Boc-Gly-(E/Z)-ΔPhe-NMe2 ) in chloroform were studied by NMR and IR spectroscopy. The experimental findings were supported by extensive calculations at DFT(B3LYP, M06-2X) and MP2 levels of theory and the β-turn tendency for both isomers of the studied dipeptide were determined in vacuum and in solution. The theoretical data and experimental IR results were used as an additional information for the NMR-based determination of the detailed solution conformations of the peptides. The obtained results reveal that N-methylation of C-terminal amide group changes dramatically the conformational properties of studied dehydropeptides. Theoretical conformational analysis reveals that the tendency to adopt β-turn conformations is much weaker for the N-methylated Z isomer (Boc-Gly-(Z)-ΔPhe-NMe2 ), both in vacuum and in polar environment. On the contrary, N-methylated E isomer (Boc-Gly-(E)-ΔPhe-NMe2 ) can easily adopt β-turn conformation, but the backbone torsion angles (φ1, ψ1, φ2, ψ2) are off the limits for common β-turn types.

show abstract

“…It has been well established that ( Z )‐ΔPhe residue has the strong tendency to stabilize β‐turns in short model peptides and 3 10 helical conformations in longer peptides 10. According to a few literature data, ( E )‐ΔPhe adopts in its crystal state the β (ϕ, ψ ∼ − 42°, 124°) conformation and the α L (ϕ, ψ ∼ 51°, 49°) conformation 11–13. In nonpolar solvents, the extended conformer C 5 (ϕ, ψ ∼ − 179°, 162°) can be also found 14…”

Section: Introductionmentioning

confidence: 99%

Experimental and theoretical NMR and IR studies of the side‐chain orientation effects on the backbone conformation of dehydrophenylalanine residue

Buczek

Ptak

Kupka

et al. 2011

Magnetic Reson in Chemistry

View full text Add to dashboard Cite

Conformation of N-acetyl-(E)-dehydrophenylalanine N', N'-dimethylamide (Ac-(E)-ΔPhe-NMe(2)) in solution, a member of (E)-α, β-dehydroamino acids, was studied by NMR and infrared spectroscopy and the results were compared with those obtained for (Z) isomer. To support the spectroscopic interpretation, the Φ, Ψ potential energy surfaces were calculated at the MP2/6-31 + G(d,p) level of theory in chloroform solution modeled by the self-consistent reaction field-polarizable continuum model method. All minima were fully optimized by the MP2 method and their relative stabilities were analyzed in terms of π-conjugation, internal H-bonds and dipole interactions between carbonyl groups. The obtained NMR spectral features were compared with theoretical nuclear magnetic shieldings, calculated using Gauge Independent Atomic Orbitals (GIAO) approach and rescaled to theoretical chemical shifts using benzene as reference. The calculated indirect nuclear spin-spin coupling constants were compared with available experimental parameters.

show abstract

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

Cited by 12 publications

References 20 publications

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

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

Toward engineering efficient peptidomimetics. Screening conformational landscape of two modified dehydroaminoacids

Experimental and theoretical NMR and IR studies of the side‐chain orientation effects on the backbone conformation of dehydrophenylalanine residue

Contact Info

Product

Resources

About