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Article: Chemical Synthesis of Proteins with Base-Labile Posttranslational Modifications Enabled by a Boc-SPPS Based General Strategy Towards Peptide C-Terminal Salicylaldehyde Esters

TitleChemical Synthesis of Proteins with Base-Labile Posttranslational Modifications Enabled by a Boc-SPPS Based General Strategy Towards Peptide C-Terminal Salicylaldehyde Esters
Authors
KeywordsBase-Labile
Boc SPPS
Chemical Protein Synthesis
Salicylaldehyde Ester
Issue Date29-Nov-2022
PublisherWiley
Citation
Angewandte Chemie International Edition, 2023, v. 62, n. 1 How to Cite?
Abstract

Chemical synthesis of proteins bearing base-labile post-translational modifications (PTMs) is a challenging task. For instance, O-acetylation and S-palmitoylation PTMs cannot survive Fmoc removal conditions during Fmoc-solid phase peptide synthesis (SPPS). In this work, we developed a new Boc-SPPS-based strategy for the synthesis of peptide C-terminal salicylaldehyde (SAL) esters, which are the key reaction partner in Ser/Thr ligation and Cys/Pen ligation. The strategy utilized the semicarbazone-modified aminomethyl (AM) resin, which could support the Boc-SPPS and release the peptide SAL ester upon treatment with TFA/H2O and pyruvic acid. The non-oxidative aldehyde regeneration was fully compatible with all the canonical amino acids. Armed with this strategy, we finished the syntheses of the O-acetylated protein histone H3(S10ac, T22ac) and the hydrophobic S-palmitoylated peptide derived from caveolin-1.


Persistent Identifierhttp://hdl.handle.net/10722/331195
ISSN
2023 Impact Factor: 16.1
2023 SCImago Journal Rankings: 5.300
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMa, WJ-
dc.contributor.authorWu, HX-
dc.contributor.authorLiu, S-
dc.contributor.authorWei, TY-
dc.contributor.authorLi, XD-
dc.contributor.authorLiu, H-
dc.contributor.authorLi, XC-
dc.date.accessioned2023-09-21T06:53:35Z-
dc.date.available2023-09-21T06:53:35Z-
dc.date.issued2022-11-29-
dc.identifier.citationAngewandte Chemie International Edition, 2023, v. 62, n. 1-
dc.identifier.issn1433-7851-
dc.identifier.urihttp://hdl.handle.net/10722/331195-
dc.description.abstract<p>Chemical synthesis of proteins bearing base-labile post-translational modifications (PTMs) is a challenging task. For instance, <em>O</em>-acetylation and <em>S</em>-palmitoylation PTMs cannot survive Fmoc removal conditions during Fmoc-solid phase peptide synthesis (SPPS). In this work, we developed a new Boc-SPPS-based strategy for the synthesis of peptide C-terminal salicylaldehyde (SAL) esters, which are the key reaction partner in Ser/Thr ligation and Cys/Pen ligation. The strategy utilized the semicarbazone-modified aminomethyl (AM) resin, which could support the Boc-SPPS and release the peptide SAL ester upon treatment with TFA/H<sub>2</sub>O and pyruvic acid. The non-oxidative aldehyde regeneration was fully compatible with all the canonical amino acids. Armed with this strategy, we finished the syntheses of the <em>O</em>-acetylated protein histone H3(S10ac, T22ac) and the hydrophobic <em>S</em>-palmitoylated peptide derived from caveolin-1.</p>-
dc.languageeng-
dc.publisherWiley-
dc.relation.ispartofAngewandte Chemie International Edition-
dc.subjectBase-Labile-
dc.subjectBoc SPPS-
dc.subjectChemical Protein Synthesis-
dc.subjectSalicylaldehyde Ester-
dc.titleChemical Synthesis of Proteins with Base-Labile Posttranslational Modifications Enabled by a Boc-SPPS Based General Strategy Towards Peptide C-Terminal Salicylaldehyde Esters-
dc.typeArticle-
dc.identifier.doi10.1002/anie.202214053-
dc.identifier.scopuseid_2-s2.0-85143292797-
dc.identifier.volume62-
dc.identifier.issue1-
dc.identifier.eissn1521-3773-
dc.identifier.isiWOS:000891934000001-
dc.identifier.issnl1433-7851-

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