tBuCO-ψ[CO-N(OH)]-Gly-NHiPr

Aubry, A.; Dupont, Virginie; Marraud, Michel

doi:10.1107/s0108270194006025

Cited by 4 publications

(5 citation statements)

References 4 publications

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“… a The values in the parentheses are from the crystal structure of an N -hydroxy peptide t BuCO-Ψ[CO−N(OH)]-Gly-NH i Pr …”

Section: Resultsmentioning

confidence: 99%

“…Aubry et al . have reported the crystal structure of a small N -hydroxy unnatural peptide t BuCO-Ψ[CO−N(OH)]-Gly-NH i Pr. The reported structure has a close resemblance to the LM of NMAOH around the N -hydoxy amide region.…”

Section: Resultsmentioning

confidence: 99%

“…It appears that the consideration of electron correlation in both There is a small increase of about 0.08-0.1 Å in the C(O)-N bond length in the transition states for rotation about the ω angle compared to the two ground states (GM and LM). Aubry et al 28 have reported the crystal structure of a small N-hydroxy unnatural peptide t BuCO-Ψ[CO-N(OH)]-Gly-NH i Pr. The reported structure has a close resemblance to the LM of NMAOH around the N-hydoxy amide region.…”

Section: Potential Energy Surface (Pes) Of Nmaoh (Ii)mentioning

confidence: 99%

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The ω, φ, and ψ Space of N-Hydroxy-N-methylacetamide and N-Acetyl-N ‘-hydroxy-N ‘-methylamide of Alanine and Their Boron Isosteres

Malde

Khedkar

Coutinho

2006

J. Chem. Theory Comput.

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The conformational space of N-hydroxy-N-methylacetamide [CH3-CO-N(OH)CH3, NMAOH] and its boron isostere [CH3-CO-B(OH)CH3, BMAOH] has been studied by quantum chemical methods. The potential energy surface of NMAOH and BMAOH has been built at the HF, B3LYP, and MP2 levels of theory with the 6-31+G* basis set. The minima and transition states for rotations about various torsional angles have been located, and the energy barriers have been estimated. The global minimum energy structure of both peptides exhibits an intramolecular hydrogen bond between the carbonyl oxygen and the hydroxyl group, imparting a conformational rigidity to the peptides. The omega rotation barrier is lower in the boron isostere than in NMAOH. The difference in the rotation barrier has been attributed to second-order orbital interactions, like negative hyperconjugation, as revealed by NBO calculations. In contrast, the rotation barrier around the torsion angle tau (torsion governing rotation about the N-O and B-O bonds) is relatively higher in the boron analogue. This difference is due to the double bond character in the B-O bond as opposed to the N-O bond which has the character of a single bond. As an extension, N-acetyl-N'-hydroxy-N'-methylamide of alanine (Ala-NOH) and its boron isostere (Ala-BOH) have been adopted as model peptides to study the conformational preferences about the φ and ψ torsion angles. The study reveals a strong preference for a Type I beta turn as well as inclinations for a left-handed alpha helix, for positive phi torsions, and for extended psi conformations for Ala-NOH; Ala-BOH, on the other hand, shows a leaning toward positive phi and extended psi, with no preference for any regular secondary structure motifs. The replacement of nitrogen by boron changes the electronic and conformational properties of the peptide, extending greater flexibility around the omega angle, a strong preference for positive phi values, and a shift in the site of nucleophilic attack from the carbonyl group to boron.

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“… a The values in the parentheses are from the crystal structure of an N -hydroxy peptide t BuCO-Ψ[CO−N(OH)]-Gly-NH i Pr …”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Potential Energy Surface (Pes) Of Nmaoh (Ii)mentioning

confidence: 99%

See 1 more Smart Citation

The ω, φ, and ψ Space of N-Hydroxy-N-methylacetamide and N-Acetyl-N ‘-hydroxy-N ‘-methylamide of Alanine and Their Boron Isosteres

Malde

Khedkar

Coutinho

2006

J. Chem. Theory Comput.

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“…The first of such structures were reported by Smith and Raymond in 1980, who found that the two hydroxamic acids in N , N ′‐dihydroxy‐ N , N ′‐diisopropylhexanediamide were trans in the solid state 64. Subsequent experimental and computational methods have shown that N ‐hydroxylated peptides exist almost exclusively as trans isomers 65–67. In addition, N ‐hydroxy peptides are known to be strong hydrogen bond donors, and the O‐H bonds in these systems have been found to extend perpendicular to the amide plane 64–66, 68.…”

Section: Introductionmentioning

confidence: 99%

“…Subsequent experimental and computational methods have shown that N ‐hydroxylated peptides exist almost exclusively as trans isomers 65–67. In addition, N ‐hydroxy peptides are known to be strong hydrogen bond donors, and the O‐H bonds in these systems have been found to extend perpendicular to the amide plane 64–66, 68. Collectively, these findings suggested that the installation of N ‐hydroxy amide side chains into peptoids could impact their local backbone conformations by both enforcing trans amides and engaging in unique hydrogen bonds.…”

Section: Introductionmentioning

confidence: 99%

Design and conformational analysis of peptoids containing N‐hydroxy amides reveals a unique sheet‐like secondary structure

et al. 2011

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N-hydroxy amides can be found in many naturally occurring and synthetic compounds and are known to act as both strong proton donors and chelators of metal cations. We have initiated studies of peptoids, or N-substituted glycines, that contain N-hydroxy amide side chains to investigate the potential effects of these functional groups on peptoid backbone amide rotamer equilibria and local conformations. We reasoned that the propensity of these functional groups to participate in hydrogen bonding could be exploited to enforce intramolecular or intermolecular interactions that yield new peptoid structures. Here, we report the design, synthesis, and detailed conformational analysis of a series of model N-hydroxy peptoids. These peptoids were readily synthesized, and their structures were analyzed in solution by 1D and 2D NMR and in the solidstate by X-ray crystallography. The N-hydroxy amides were found to strongly favor trans conformations with respect to the peptoid backbone in chloroform. More notably, unique sheetlike structures held together via intermolecular hydrogen bonds were observed in the X-ray crystal structures of an N-hydroxy amide peptoid dimer, which to our knowledge represent the first structure of this type reported for peptoids. These results suggest that the N-hydroxy amide can be utilized to control both local backbone geometries and longer-range intermolecular interactions in peptoids, and represents a new functional group in the peptoid design toolbox.

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Peptide N‐Amination Supports β‐Sheet Conformations

et al. 2017

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The conformational heterogeneity of backbone Nsubstituted peptides limits their ability to adopt stable secondary structures.H erein, we describe ap ractical synthesis of backbone aminated peptides that readily adopt b-sheet folds. Data derived from model N-amino peptides suggest that extended conformations are stabilized through cooperative steric, electrostatic,and hydrogen-bonding interactions.

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tBuCO-ψ[CO-N(OH)]-Gly-NHiPr

Cited by 4 publications

References 4 publications

The ω, φ, and ψ Space of N-Hydroxy-N-methylacetamide and N-Acetyl-N ‘-hydroxy-N ‘-methylamide of Alanine and Their Boron Isosteres

The ω, φ, and ψ Space of N-Hydroxy-N-methylacetamide and N-Acetyl-N ‘-hydroxy-N ‘-methylamide of Alanine and Their Boron Isosteres

Design and conformational analysis of peptoids containing N‐hydroxy amides reveals a unique sheet‐like secondary structure

Peptide N‐Amination Supports β‐Sheet Conformations

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