A New Method for the Protection of the Sulfhydryl Group during Peptide Synthesis

Akabori, Shirô; Sakakibara, Shumpei; Shimonishi, Yasutsugu; Nobuhara, Yoshifumi

doi:10.1246/bcsj.37.433

Cited by 64 publications

(20 citation statements)

References 2 publications

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“…To protect the phenolic function of Tyr, 346 both the amino and carboxylic groups must be protected either by forming a copper (II) chelate or using orthogonal protecting groups. t Bu-protected Tyr is obtained using isobutylene in acidic medium, 418 whereas with the other Tyr-protected derivatives the corresponding alkyl halide is used as the protecting agent.…”

Section: Introduction Of the Protecting Groupsmentioning

confidence: 99%

Amino Acid-Protecting Groups

2009

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Section: Introduction Of the Protecting Groupsmentioning

confidence: 99%

Amino Acid-Protecting Groups

2009

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“…Fmoc-protected Cys is also commercially available at reasonable cost with methoxybenzyl (Mob) protection on the cysteine. [40] The methoxybenzyl group can be removed from Cys with extended time or elevated temperature using standard TFA/TIS/H 2 O peptide cleavage/deprotection conditions. [39,41,42] Thus, we examined whether the Mob-protected Fmoc-cysteine (Fmoc-Cys(Mob)-OH, 3) might be an appropriate starting material for the synthesis of peptides with cysteine sulfinic acid.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of peptides with cysteine sulfinic acid via the cysteine methoxybenzyl sulfone

Urmey

Zondlo

2019

Peptide Science

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Cysteine sulfinic acid is a protein posttranslational modification that is formed under oxidative conditions and is regulated both enzymatically and nonenzymatically. Cysteine oxidation to the sulfinic acid has been observed broadly throughout the proteome and can induce activation or inhibition of function in proteins. Recently, wide‐scale, reversible regulation of the sulfinic acid state of cysteine within proteins was identified, posing new questions in cysteine sulfinic acid biology. Existing methods to synthesize peptides with cysteine sulfinic acid can suffer from low yield, due to the formation of side products in the disulfide, sulfenic acid, and/or sulfonic acid oxidation states. Herein, a method for the synthesis of peptides with cysteine sulfinic acids was developed, via protection of cysteine sulfinic acid as the methoxybenzyl (Mob) sulfone. Cysteine Mob sulfone was synthesized as an Fmoc amino acid in one step from the commercially available Mob‐protected Fmoc‐cysteine (Fmoc‐Cys(Mob)‐OH). This amino acid was directly incorporated into peptides via solid‐phase peptide synthesis. Alternatively, peptides were synthesized using Fmoc‐Cys(Mob)‐OH, followed by subsequent oxidation within peptides of the thioether to the Mob sulfone via H2O2 and catalytic niobium carbide. Deprotection of peptides under strongly acidic conditions (50% triflic acid, 45% trifluoroacetic acid, 5% water) generated peptides with cysteine sulfinic acid. This approach was applied to the synthesis of peptides containing cysteine sulfinic acid within diverse peptide sequence contexts.

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“…Therefore, the selective protecting group elimination is possible, depending on the acidic conditions used. As a result of years of studies in the field, there are several Cys protecting groups available; some of them are labile in low acid concentration such as Mmt [8], Trt [9][10][11] or Thp [12,13]; others are more stable in low concentrations of trifluoroacetic acid (TFA) but cleavable using higher quantity of TFA -Diphenylmethyl (Dpm) [9,11,14], tBu [15,16] or MBom [17] and moreover, there are groups which are completely stable to TFA and removable using harsh conditions such as HF, for example Bom [18], Meb or Mob [19][20][21] groups.…”

Section: Acid-labile Cys Protecting Groupsmentioning

confidence: 99%