3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides

Ingole, Tukaram S.; Kotmale, Amol S.; Gawade, Rupesh L.; Gonnade, Rajesh G.; Rajamohanan, Pattuparambil R.; Sanjayan, Gangadhar J.

doi:10.1039/c6nj01667g

Cited by 2 publications

(2 citation statements)

References 45 publications

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“…The small coefficients of

H \binom{N}{A}

(−2.5 ppb/K) and

H \binom{' N}{A}

(−2.6 ppb/K) indicate that neither one is intramolecularly H‐bonded. Additionally, solvent polarity titration (CDCl 3 /[D 6 ]DMSO) showed a little variance of

H \binom{N}{iBu}

chemical shift (<0.22 ppm) with increasing fraction of [D 6 ]DMSO (Figure 2b), revealing its involvement in a strong intramolecular H‐bond, that resists solvation by competing polar solvent [29,30] . In contrast, the

H \binom{' N}{iBu}

signal showed a sharp downfield shift, similar to the solvent‐exposed amide hydrogen (

H \binom{N}{2}

) in the model compound A , which cannot form any intramolecular H‐bond.…”

Section: Figurementioning

confidence: 99%

Hydrogen Bond Surrogate‐Constrained Dynamic Antiparallel β‐Sheets

et al. 2021

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Antiparallel β‐sheets are important secondary structures within proteins that equilibrate with random‐coil states; however, little is known about the exact dynamics of this process. Here, the first dynamic β‐sheet models that mimic this equilibrium have been designed by using an H‐bond surrogate that introduces constraint and torque into a tertiary amide bond. 2D NMR data sufficiently reveal the structure, kinetics, and thermodynamics of the folding process, thereby leading the way to similar analysis in isolated biologically relevant β‐sheets.

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“…The small coefficients of

H \binom{N}{A}

(−2.5 ppb/K) and

H \binom{' N}{A}

(−2.6 ppb/K) indicate that neither one is intramolecularly H‐bonded. Additionally, solvent polarity titration (CDCl 3 /[D 6 ]DMSO) showed a little variance of

H \binom{N}{iBu}

H \binom{' N}{iBu}

signal showed a sharp downfield shift, similar to the solvent‐exposed amide hydrogen (

H \binom{N}{2}

) in the model compound A , which cannot form any intramolecular H‐bond.…”

Section: Figurementioning

confidence: 99%

Hydrogen Bond Surrogate‐Constrained Dynamic Antiparallel β‐Sheets

et al. 2021

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“…Earlier, we have reported that proline‐aminothiophene carboxylate dipeptide motifs (Pro‐Atc) n can generate conformationally constrained peptide structures (Figure ) . The presence of constrained aromatic β‐amino acid Atc was shown to assist in rigidifying the peptide backbone …”

Section: Figurementioning

confidence: 99%

Rigid Peptide Scaffold‐Incorporated Structural Analogs of the Potent Antidepressant Peptide Drug Rapastinel (GLYX‐13)

et al. 2017

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Abstract:Rapastinel (GLYX‐13) is a natural amidated tetrapeptide (Thr‐Pro‐Pro‐Thr‐NH2)endowed with strong antidepressant property. Rapastinel shows considerable promise for treating drug‐resistant major depressive disorder (MDD), and is under clinical phase III development. Herein, we report the synthesis of a novel class of analogues of the potent antidepressant peptide drug rapastinel featuring rigid dipeptide scaffolds comprising proline (L/D) and amino thiophene carboxylates (Atc). Amino thiophene carboxylate is a conformationally constrained aromatic β‐amino acid, known to rigidify peptide backbones thereby limiting the conformational flexibility of peptides and improving proteolytic stability.

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3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides

Abstract: This article demonstrates the consequences of incorporating a constrained β-amino acid into a peptide chain and its effect on conformation of oligomers.

Cited by 2 publications

References 45 publications

Hydrogen Bond Surrogate‐Constrained Dynamic Antiparallel β‐Sheets

Hydrogen Bond Surrogate‐Constrained Dynamic Antiparallel β‐Sheets

Rigid Peptide Scaffold‐Incorporated Structural Analogs of the Potent Antidepressant Peptide Drug Rapastinel (GLYX‐13)

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