Lanthionine Formation in Keratin

Earland, Christopher; Raven, David J.

doi:10.1038/191384a0

Cited by 16 publications

(5 citation statements)

References 4 publications

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“…The breaking of the cystine disulphide bond usually occurs after treatment with reducing agents or strongly basic solutions. In this latter case, after approximately 10–15 min at room temperature, the lanthionization can take place with formation of a covalent thioether bond ; such an event seems improbable upon treatment with carbonyl compounds due to the semipermanent character of the straightening conferred by this technique. In addition, the breaking of the cystine disulphide bond causes a weakening of the hair fibre, and also, this contrasts with its healthy appearance and shiny aspect after the straightening; this might be another indication of the non‐occurrence of the S–S bond rupture upon treatment with aldehydes.…”

Section: Resultsmentioning

confidence: 99%

Formaldehyde replacement with glyoxylic acid in semipermanent hair straightening: a new and multidisciplinary investigation

Boga

Taddei

Micheletti

et al. 2014

Intern J of Cosmetic Sci

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This investigation revealed the role played by the electrophilicity of the carbonyl on the straightener agent and of the temperature, closely related to the dehydration process. Raman and IR studies indicated the involvement of imine bonds and the occurrence of a sequence of conformational modifications during the straightening procedure. SEM analyses showed the effectiveness of the treatment at the cuticular level.

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Section: Resultsmentioning

confidence: 99%

Formaldehyde replacement with glyoxylic acid in semipermanent hair straightening: a new and multidisciplinary investigation

Boga

Taddei

Micheletti

et al. 2014

Intern J of Cosmetic Sci

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“…[10] The elimination mechanism of one of the sulfur atoms of the disulfide bond of the cysteine, leading to the formation of a thioether, was described by Earland and Raven. [11] Lanthionines are also commonly found in lantibiotics, a group of antimicrobial peptides that contains also several other modified amino acids. [12,13] Given the fact that lanthionine was first isolated from sodium-carbonate-treated wool, it may be hypothesised that the formation of this variant may be favoured by alkaline pH and elevated temperatures.…”

Section: Discussionmentioning

confidence: 99%

Characterisation of a Novel Growth Hormone Variant Comprising a Thioether Link between Cys182 and Cys189

et al. 2007

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A novel variant of recombinant human growth hormone (r-hGH), isolated from biopharmaceutical preparations produced in E. coli, was identified and characterised. This variant contains a nonreducible thioether bridge near the C terminus between Cys182 and Cys189 and was characterised using various analytical techniques. As previous work by Cunningham and Wells (1993) highlighted the involvement of several residues in this part of the sequence in the binding and affinity of the molecule to its receptor, the presence of this modified intramolecular link may have important implications with regard to the biological behaviour of the molecule. Furthermore, as the conversion of a disulfide into a thioether was previously reported for a therapeutic monoclonal antibody (Tous et al., 2005), this may imply that disulfide bridges located in this part of the molecule have a generic susceptibility to thioether formation. This in turn is relevant to the biopharmaceutical industry for monitoring the integrity of disulfide bridges near the protein C terminus. The present study exhibits a state of the art physicochemical investigation for the unequivocal elucidation of a novel structure involving peptide mapping with mass spectrometry and de novo peptide sequencing. Changes in the higher order structure of the molecule were highlighted by near UV circular dichroism and molecular modelling.

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“…Under appropriate conditions, a disulfide bond can undergo reversible ␤-elimination, transforming a cysteine residue into dehydroalanine. This species is relatively unstable and susceptible to nucleophilic attack by an adjacent cysteine residue to form a thioether bond (32)(33)(34) or reformation of the disulfide. Reformation of the disulfide bond also results in rehydrogenation and can be observed by deuterium incorporation on the cysteine (Ref.…”

Section: Discussionmentioning

confidence: 99%

IgG1 Thioether Bond Formation in Vivo

Zhang

Schenauer

McCarter

et al. 2013

Journal of Biological Chemistry

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Background: Thioethers have been observed in therapeutic antibodies, with increasing levels upon storage. Results: IgG1 thioether bond formation is naturally occurring, but the formation rate depends on light chain type. Conclusion: Slower thioether bond formation on IgG1 is caused by dehydrogenation impairment through its light chain. Significance: Safety concerns associated with thioether control on therapeutic antibodies are diminished by its natural production.

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Lanthionine Formation in Keratin

Cited by 16 publications

References 4 publications

Formaldehyde replacement with glyoxylic acid in semipermanent hair straightening: a new and multidisciplinary investigation

Formaldehyde replacement with glyoxylic acid in semipermanent hair straightening: a new and multidisciplinary investigation

Characterisation of a Novel Growth Hormone Variant Comprising a Thioether Link between Cys182 and Cys189

IgG1 Thioether Bond Formation in Vivo

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