A Comprehensive Approach to the Synthesis of Sulfate Esters

Simpson, Levi S.; Widlanski, Theodore S.

doi:10.1021/ja056086j

Cited by 124 publications

(119 citation statements)

References 21 publications

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“…To determine IC 50 values for C4-derived peptides, all proteins and peptides were tested at a final molar ratio of 1 3 ], which was prepared and introduced to the growing peptide chain using the method described previously (25,26 2 ) C4 peptides were synthesized by GL Biochem using Fmoc-strategy solidphase peptide synthesis. The modified and unmodified peptides were used at final concentrations of 5-500 mM.…”

Section: Measurement Of the Cleavage Of C4 By Protease Variantsmentioning

confidence: 99%

Identification of a Catalytic Exosite for Complement Component C4 on the Serine Protease Domain of C1s

Duncan

Mohlin

Taleski

et al. 2012

The Journal of Immunology

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The classical pathway of complement is crucial to the immune system, but it also contributes to inflammatory diseases when dysregulated. Binding of the C1 complex to ligands activates the pathway by inducing autoactivation of associated C1r, after which C1r activates C1s. C1s cleaves complement component C4 and then C2 to cause full activation of the system. The interaction between C1s and C4 involves active site and exosite-mediated events, but the molecular details are unknown. In this study, we identified four positively charged amino acids on the serine protease domain that appear to form a catalytic exosite that is required for efficient cleavage of C4. These residues are coincidentally involved in coordinating a sulfate ion in the crystal structure of the protease. Together with other evidence, this pointed to the involvement of sulfate ions in the interaction with the C4 substrate, and we showed that the protease interacts with a peptide from C4 containing three sulfotyrosine residues. We present a molecular model for the interaction between C1s and C4 that provides support for the above data and poses questions for future research into this aspect of complement activation.

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Section: Measurement Of the Cleavage Of C4 By Protease Variantsmentioning

confidence: 99%

Identification of a Catalytic Exosite for Complement Component C4 on the Serine Protease Domain of C1s

Duncan

Mohlin

Taleski

et al. 2012

The Journal of Immunology

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“…An alternative strategy based on the use of the protected sulfonation reagent 8 [25,26] was investigated [27,28]. Following the procedure of Taylor [29], treatment of phenol 7 (0.3 M concentration in the reaction medium) with an excess of 8 in the presence of triethylamine and DMAP afforded the sulfate diester 10 in 94% yield.…”

Section: Synthesis Of Sulfated Metanephrinesmentioning

confidence: 99%

Synthetic calibrators for the analysis of total metanephrines in urine: Revisiting the conditions of hydrolysis

Simonin

Gerber‐Lemaire

Centeno

et al. 2012

Clinica Chimica Acta

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Background: The quantification of total (free + sulfated) metanephrines in urine is recommended to diagnose pheochromocytoma. Urinary metanephrines include metanephrine itself, normetanephrine and methoxytyra-mine, mainly in the form of sulfate conjugates (60-80%). Their determination requires the hydrolysis of the sul-fate ester moiety to allow electrochemical oxidation of the phenolic group. Commercially available urine calibrators and controls contain essentially free, unhydrolysable metanephrines which are not representative of native urines. The lack of appropriate calibrators may lead to uncertainty regarding the completion of the hy-drolysis of sulfated metanephrines, resulting in incorrect quantification. Methods: We used chemically synthesized sulfated metanephrines to establish whether the procedure most fre-quently recommended for commercial kits (pH 1.0 for 30 min over a boiling water bath) ensures their complete hydrolysis. Results: We found that sulfated metanephrines differ in their optimum pH to obtain complete hydrolysis. Highest yields and minimal variance were established for incubation at pH 0.7-0.9 during 20 min. Conclusion: Urinary pH should be carefully controlled to ensure an efficient and reproducible hydrolysis of sul-fated metanephrines. Synthetic sulfated metanephrines represent the optimal material for calibrators and pro-ficiency testing to improve inter-laboratory accuracy.

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“…66,70 To overcome some of these problems, which also complicate the synthesis of other biologically relevant sulfate esters such as sulfated oligosaccharides and steroids, Simpson and Widlanski recently developed a general strategy for the synthesis of sulfate monoesters using alkyl protecting groups. 81 The authors found that neopentyl protected sulfate monoesters are exceptionally stable under strongly acidic and basic conditions, and they demonstrated that the neopentyl group can be quantitatively removed with sodium azide in dimethylformamide (DMF). They also described the preparation of Fmoc and Boc derivatives of neopentyl-protected sulfoTyr, emphasizing the potential usefulness of this strategy for solid-phase synthesis of sulfoTyr peptides.…”

Section: 74mentioning

confidence: 99%

Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine‐containing peptides

2008

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A Comprehensive Approach to the Synthesis of Sulfate Esters

Cited by 124 publications

References 21 publications

Identification of a Catalytic Exosite for Complement Component C4 on the Serine Protease Domain of C1s

Identification of a Catalytic Exosite for Complement Component C4 on the Serine Protease Domain of C1s

Synthetic calibrators for the analysis of total metanephrines in urine: Revisiting the conditions of hydrolysis

Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine‐containing peptides

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