Thioamides in the collagen triple helix

Newberry, Robert W.; VanVeller, Brett; Raines, Ronald T.

doi:10.1039/c5cc02685g

Cited by 71 publications

(70 citation statements)

References 58 publications

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“…The PP S G modification shows a stabilization of the triple helix with a significant increase in T m and 0.4 kcal mol –1 increase in Δ G U , while PPG S shows a moderate destabilization, in agreement with previous studies. 24 Hysteresis studies showed that the free energy differences are in good agreement with the melting temperature profiles (Fig. S32–S36†).…”

Section: Resultssupporting

confidence: 54%

The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts

et al. 2017

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Section: Resultssupporting

confidence: 54%

The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts

et al. 2017

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“…The intramolecular O…CO distance should be less than 3.2 Å and the corresponding bond angle 100°–120°. More recently, Raines and coworkers extended this investigation to endothioxopeptides (through the detailed NMR determination of their trans / cis ratios) and others to endothioxopeptoids. In the former compounds, theoretical analyses demonstrated that the energy of the n → π * interaction is higher when the donor atom is sulfur (as compared to oxygen).…”

Section: Resultsmentioning

confidence: 99%

Endothioxopeptides: A conformational overview

et al. 2016

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Although thionamides would have been first prepared two centuries ago and their chemical and spectroscopic properties extensively investigated, only much more recently (since about 1985) a well deserved but still insufficient attention has been paid to their endothioxopeptide subfamily which nonetheless currently represents a rapidly emerging area of great scientific interest in the broader field of foldameric compounds based on biologically relevant building blocks. After two brief sections offering information on the unfortunately still limited number of endothioxopeptides discovered from natural sources but also on the impressive advancements registered in the last few years in their synthetic methods, this review article outlines the results of a detailed literature survey on the ongoing great, but not systematic, progress related to the conformational consequences generated by incorporating one (or more) thionamide group(s) into a polypeptide chain. Finally, a short discussion of the growing, but still in its infancy, class of the endoselenoxopeptide congeners is also presented.

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“…Thioamides mimic the shape and structure of peptide bonds but present different electronic and hydrogen-bonding properties-making thioamides important biophysical probes of peptide structure and function. 1,2 For example, thioamides have been employed to interrogate hydrogen-bonding in α-helices and β-turn structures, [3][4][5] as well as n→π* interactions between peptides bonds across amino acids (i → i + 1). [6][7][8] Further, thioamides have been applied in photochemical isomerization schemes, 9,10 and can serve as quenchers of fluorescent probes to study peptide folding.…”

Section: Introductionmentioning

confidence: 99%

Deprotection Strategies for Thioimidates During Fmoc Solid-Phase Peptide Synthesis: A Safe Route to Thioamides

Camacho¹,

Nguyen²,

Turner³

et al. 2019

Preprint

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Thioamides are important biophysical probes of peptide folding, but are prone to α-C epimerization during Fmoc solid-phase peptide synthesis. The stereochemical integrity of thioamide-containing peptides can be dramatically improved by protecting the thioamide as a thioimidate during synthesis. A drawback of this approach, however, is that once synthesis of the peptide is complete, regeneration of the thioamide requires the toxic, corrosive, and flammable gas H2S. This work examines several approaches to supplant H2S as a deprotection reagent in favor of a safer and more convenient alternative. Ultimately, a new application of the 4-azidobenzyl protecting group to thioamides was found to provide the most suitable means of both protection of α-C stereochemistry and conversion back to thioamide.

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Thioamides in the collagen triple helix

Cited by 71 publications

References 58 publications

The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts

The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts

Endothioxopeptides: A conformational overview

Deprotection Strategies for Thioimidates During Fmoc Solid-Phase Peptide Synthesis: A Safe Route to Thioamides

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