The crystal structure of N-[[6-methoxy-5-(trifluoromethyl)thio-1-naphthalenyl]thioxomethyl]-N-methylglycine, C16H14F3NO3S2

Varughese, Kottayil I.; Przybylska, M.; Sestanj, K.; Bellini, F.; Humber, Leslie G.

doi:10.1139/v83-371

Cited by 14 publications

(6 citation statements)

References 5 publications

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“…In the myotropic assay, the analog retained in the ground state 80% of the maximal response obtained with the parent kinin pentapeptide (Table 1). This slight activity loss may result from the larger size of the sulfur atom [42,43], the longer carbon-sulfur bond length [44,45], and the different electron distribution of thioxopeptide bond ψ[CS-N] [46]. In the photostationary state, a fourfold enhanced myotropic activity was observed.…”

Section: Discussionmentioning

confidence: 99%

A photoswitchable thioxopeptide bond facilitates the conformation‐activity correlation study of insect kinin

Huang

Cong

Yang

et al. 2008

Journal of Peptide Science

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Thioxopeptide bond psi[CS-N], a nearly isosteric modification of the native peptide bond, was introduced into insect kinin active core pentapeptide to evaluate the impact of backbone cis/trans photoswitching on bioactivity. The thioxo analog Phe(1)-Tyr(2)-psi[CS-N]-Pro(3)-Trp(4)-Gly(5)-NH(2) (psi[CS-N](2)-kinin), was synthesized by Fmoc solid-phase peptide strategy. The reversible photoswitching property was characterized via spectroscopic methods and HPLC, which showed that the cis conformer increased from 15.7 to 47.7% after 254 nm UV irradiation. A slow thermal reisomerization (t(1/2) = 40 min) permitted us to determine the cockroach hindgut myotropic activity of the thioxopeptide in the photostationary state. The results indicated that the activity increased significantly after UV irradiation and recovered to the ground level after thermal re-equilibration. In the present study, by utilizing the phototriggered isomerization in a specific position of peptide backbone, we revealed that the cis psi[CS-N](2)-kinin conformer is the active conformation when interacting with kinin receptor on cockroach hindgut.

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Section: Discussionmentioning

confidence: 99%

A photoswitchable thioxopeptide bond facilitates the conformation‐activity correlation study of insect kinin

Huang

Cong

Yang

et al. 2008

Journal of Peptide Science

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“…Bond lengths and angles are listed in Table 2. Like other inhibitors of aldose reductase (Varma, Mikuni & Kinoshita, 1975;Kador, Sharpless & Goosey, 1982;Varughese, Przybylska, Sestani, Bellini & Humber, 1983), the sorbinil molecule contains a large planar aromatic region. The fragment of the molecule containing the phenyl ring and atoms O(1) and C(4) is essentially planar (largest deviation of an atom from the least-squares plane 0.02 A).…”

Section: Experimental Sample Of Sorbinil Provided By Pfizermentioning

confidence: 99%

Crystal structure of sorbinil, C11H9FN2O3

Kissinger¹,

Adman²,

Clark³

et al. 1985

Acta Crystallogr C

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Abstract. Mr= 236.12, orthorhombic, P2~212 ~, a = 7.5096 (6), (1), c--21.018 (3) A, V= 1009.7 (3) A 3, Z = 4, D x = 1.552 gcm -3, ,~(Cu Ka) =1.54178A, ~=4.77cm -1, F(000)=488, T= 293 K, final R =0.042 for 749 unique observed reflections. The molecule contains fluorobenzene and hydantoin rings connected via a nonplanar pyran ring. The obtuse angle between the planes of the fluorobenzene and hydantoin rings is 98 °. Bond distances and angles are normal except for CH2-CH 2 of the pyran ring which at 1.484 (8)A is 0.057 A shorter than the standard value.

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“…Several structural changes upon going from amides to thioamides have been observed. The thioamide rotational barrier about the CSNH bond is approximately 8–12 kJ mol –1 larger than that for the amide (CONH) bond due to the more pronounced double bond character of the thiopeptide CN bond. , The longer CS double bond (1.64 Å) in comparison with the CO bond (1.24 Å), , as well as the larger covalent and van der Waals radii of sulfur, and modified hydrogen-bond-accepting abilities of thioamides affect the overall changes in the conformational behavior of thioamide-containing molecules. Some very recent studies have investigated the thioamide backbone in peptoids containing aromatic side chains. , These studies outlined earlier reported findings of the importance of n → π* interactions, characterized by the donation of electron density from the thiocarbonyl sulfur lone pair to the π* orbital of an adjacent amide carbonyl, in stabilization of the trans -amide conformation in a peptide chain .…”

Section: Introductionmentioning

confidence: 99%

Conformational Features of Thioamide-Containing Dipeptoids and Peptoid–Peptide Hybrids—Computational and Experimental Approaches

Zimnicka

2018

J. Phys. Chem. A

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The effects of thioamide incorporation into N, N-dimethyl-2-( N-methylacetamido)acetamide and N-methyl-2-( N-methylacetamido)acetamide as the simplest models of a dipeptoid structure and a peptoid-peptide hybrid are discussed. The solvent-modulated conformational features of model compounds were examined by computations enhanced by natural bond orbital (NBO) analysis and experimentally by kinetic and equilibrium measurements using NMR spectroscopy. The computations supported by NBO analysis showed that intrinsic stability of the predominant trans isomer (α and C forms) of the dipeptoid model results from an indirect n → π* interaction, occurring between the carbonyl oxygen lone pair ( n) and the π* orbital of the adjacent amide carbonyl through the C-H antibond (σ*). The direct n → π* interaction constitutes a negligible contribution to trans stabilization. The N-terminal thioxo substitution increases this indirect electron delocalization, making the α isomer prevalent. The n → σ* interaction is an additional source of stability of the trans-C form relevant for the underivatized dipeptoid model and its C-terminal thioamide counterpart. In the peptoid-peptide hybrid, the trans preference is perturbed by subtle differences in the H-bond donor-acceptor abilities between the thioxo and oxo groups. The cis isomer becomes more populated with an increase in the strength of polarity and the hydrogen bonding acceptor ability of the solvent molecules. While thioxo substitution slightly shifts the trans- cis equilibrium in polar solvents, it effectively allows for increasing or decreasing the barrier to trans- cis rotation with respect to underivatized model compounds depending on N- vs C-terminal thioamide backbone substitution.

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The crystal structure of N-[[6-methoxy-5-(trifluoromethyl)thio-1-naphthalenyl]thioxomethyl]-N-methylglycine, C₁₆H₁₄F₃NO₃S₂

Cited by 14 publications

References 5 publications

A photoswitchable thioxopeptide bond facilitates the conformation‐activity correlation study of insect kinin

A photoswitchable thioxopeptide bond facilitates the conformation‐activity correlation study of insect kinin

Crystal structure of sorbinil, C11H9FN2O3

Conformational Features of Thioamide-Containing Dipeptoids and Peptoid–Peptide Hybrids—Computational and Experimental Approaches

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