Sulfur-containing polypeptides. X. .beta.-Elimination of mercaptides from cysteine peptides

Hiskey, Richard G.; Upham, Roger A.; Beverly, G. M.; Jones, Warren Chandler

doi:10.1021/jo00827a053

Cited by 20 publications

(4 citation statements)

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“…Noteworthy, no racemization of the chiral center was observed (see Supporting Information, pp S33–S34 and Figure S48). In contrast, base-catalyzed hydrolysis of 1p does not only deprotect the ester group, but also causes elimination of the RS- group, forming olefinic side products . Significantly, this result indicates that the current system for selective hydrogenation of thioesters can serve as a deprotection strategy for the thiol group.…”

mentioning

confidence: 99%

Catalytic Hydrogenation of Thioesters, Thiocarbamates, and Thioamides

et al. 2020

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Direct hydrogenation of thioesters with H2 provides a facile and waste-free method to access alcohols and thiols. However, no report of this reaction is documented, possibly because of the incompatibility of the generated thiol with typical hydrogenation catalysts. Here, we report an efficient and selective hydrogenation of thioesters. The reaction is catalyzed by an acridine-based ruthenium complex without additives. Various thioesters were fully hydrogenated to the corresponding alcohols and thiols with excellent tolerance for amide, ester, and carboxylic acid groups. Thiocarbamates and thioamides also undergo hydrogenation under similar conditions, substantially extending the application of hydrogenation of organosulfur compounds.

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confidence: 99%

Catalytic Hydrogenation of Thioesters, Thiocarbamates, and Thioamides

et al. 2020

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“…Hen egg-white lysozyme, a 129-amino acid polypeptide (14.3 kDa) containing four disulfide bridges, was selected for conversion into S-phosphorylated derivatives. The concept of transformation was inspired by an early work (Hiskey et al 1970) reporting the partial β-elimination of benzyl thiolate from S-benzylated cysteine peptides. Thus, it was assumed that polypeptides bearing cysteine residue S-protected by other simple alkyl groups might also produce β-elimination products in amounts detectable by modern mass spectrometry.…”

Section: Transformation Of Lysozyme Into S-phosphocysteine-containingmentioning

confidence: 99%

Modified cysteine S-phosphopeptide standards for mass spectrometry-based proteomics

Buchowiecka

2019

Amino Acids

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The regulatory role of protein cysteine phosphorylation is an under-researched area. The difficulty of accessing reference S-phosphorylated peptides (pCys-peptides) hampers progress in MS-driven cysteine phosphoproteomics, which requires targeted analytical procedures. This work describes an uncomplicated process for the conversion of disulfide-bridged protein into a complex model mixture of combinatorially modified peptides. Hen egg-white lysozyme was reduced with tris(2carboxyethyl)phosphine (TCEP) followed by alkylation of cysteine with (3-acrylamidopropyl)trimethyl-ammonium chloride (APTA) and subsequent beta-elimination in aqueous Ba(OH) 2 to yield modified polypeptides containing multiple dehydroalanine (Dha) residues. The conjugate addition of thiophosphoric acid to Dha residues followed by trypsinolysis led to numerous D/L phosphocysteine-containing peptides, which were identified by higher-energy collisional-dissociation tandem mass spectrometry (HCD-MS/MS). Our results show that some pCys-peptides produce prominent neutral losses of 80 Da, 98 Da and a weak 116 Da loss. These are similar to the neutral-loss triplets generated by phosphohistidine peptides.

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“…Peptide derivatives (I) and (11) were prepared following the prescribed mixed anhydride procedure of Anderson (7) and coupling of Z-y Abu-OH was effected by diethyl phosphorocyanidate (DEPC) according to Yamada et al (8). Peptide derivatives (I) and (11) were prepared following the prescribed mixed anhydride procedure of Anderson (7) and coupling of Z-y Abu-OH was effected by diethyl phosphorocyanidate (DEPC) according to Yamada et al (8).…”

Section: Synthesis and Purificationmentioning

confidence: 99%

DNA‐binding compounds – synthesis and intercalating properties of a peptide‐diamino diacridine

Kelly

Mack

Martin³

et al. 1985

International Journal of Peptide and Protein Research

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A novel diacridine has been prepared in which two acridines are linked by a flexible peptide chain composed of y-aminobutyric acid, tyrosine, lysine and glycine. Synthesis of N-(( 9-acridinyI)-4-aminobutanoyl-tyrosyl-lysyl-lysyl-glycyl)hf-(9-acridinyl)-l,3-diaminopropane (VII) was achieved in 8% overall yield by a solution phase stepwise procedure. This compound binds to DNA by intercalation of both chromophores with at least a 140-fold enhancement of affinity compared to 9aminoacridine.

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Sulfur-containing polypeptides. X. .beta.-Elimination of mercaptides from cysteine peptides

Cited by 20 publications

References 1 publication

Catalytic Hydrogenation of Thioesters, Thiocarbamates, and Thioamides

Catalytic Hydrogenation of Thioesters, Thiocarbamates, and Thioamides

Modified cysteine S-phosphopeptide standards for mass spectrometry-based proteomics

DNA‐binding compounds – synthesis and intercalating properties of a peptide‐diamino diacridine

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