Chemoselective protection of thiols versus alcohols and phenols. The Tosvinyl group

Arjona, Odón; Medel, Rocı́o; Rojas, Jenny; Costa, Anna M.; Vilarrasa, Jaume

doi:10.1016/s0040-4039(03)01614-9

Cited by 28 publications

(13 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Reactions of thiols with electron deficient acetylenes have been known for decades, being, however, mostly conducted in organic solvents. [421][422][423][424][425] Several examples of reactions in aqueous media have been recently reported. 417,420,426,427 Che and co-workers 417 have elaborated a versatile method for the selective cysteine labelling of unprotected peptides and proteins in aqueous media with arylalkynone reagents.…”

Section: Fig 20mentioning

confidence: 99%

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

2015

View full text Add to dashboard Cite

Bioconjugation methodologies have proven to play a central enabling role in the recent development of biotherapeutics and chemical biology approaches. Recent endeavours in these fields shed light on unprecedented chemical challenges to attain bioselectivity, biocompatibility, and biostability required by modern applications. In this review the current developments in various techniques of selective bond forming reactions of proteins and peptides were highlighted. The utility of each endogenous amino acid-selective conjugation methodology in the fields of biology and protein science has been surveyed with emphasis on the most relevant among reported transformations; selectivity and practical use have been discussed.

show abstract

Section: Fig 20mentioning

confidence: 99%

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

2015

View full text Add to dashboard Cite

show abstract

“…For many decadest he reactivity of electron deficient acetylenes with thiols hasb een explored both in organic [68][69][70] and Scheme17. Application of diarylthiomaleimidesint he generation of peptideconjugates for therapy and study of biological systems.…”

Section: Arylpropionitrilesmentioning

confidence: 99%

“…For many decades the reactivity of electron deficient acetylenes with thiols has been explored both in organic and aqueous media . In particular, alkynoic amides have been used as irreversible inhibitors of EGFR, while arylalkynones have been advanced as selective reagents for cysteine functionalization, exploiting the interchangeability of the resulting vinyl sulfide linkage .…”

Section: Other Chemical Approaches For Maleimide‐like Bioconjugationmentioning

confidence: 99%

Bioconjugation with Maleimides: A Useful Tool for Chemical Biology

Ravasco

Faustino

Trindade

et al. 2018

Chemistry A European J

378

374

View full text Add to dashboard Cite

Maleimide chemistry stands out in the bioconjugation toolbox by virtue of its synthetic accessibility, excellent reactivity, and practicability. The second-generation of clinically approved antibody-drug conjugates (ADC) and much of the current ADC pipeline in clinical trials contain the maleimide linkage. However, thiosuccinimide linkages are now known to be less robust than once thought, and ergo, are correlated with suboptimal pharmacodynamics, pharmacokinetics, and safety profiles in some ADC constructs. Rational design of novel generations of maleimides and maleimide-type reagents have been reported to address the shortcomings of classical maleimides, allowing for the formation of robust bioconjugate linkages. This review highlights the main strategies for rational reagent design that have allowed irreversible bioconjugations in cysteines, reversible labelling strategies and disulfide re-bridging.

show abstract

“…The selectivity and efficiency of the conjugation was demonstrated by the enrichment of cysteine‐containing peptides in a solution containing peptides with and without cysteine residues. Previously, the corresponding reactions of electron‐deficient alkynes had been carried out with “simple” thiols (namely cysteine and glutathione) in the presence of organic solvent …”

Section: Thiol‐ene and Thiol‐yne Reactionsmentioning

confidence: 99%

Chemical Protein Modification through Cysteine

2016

View full text Add to dashboard Cite

The modification of proteins with non-protein entities is important for a wealth of applications, and methods for chemically modifying proteins attract considerable attention. Generally, modification is desired at a single site to maintain homogeneity and to minimise loss of function. Though protein modification can be achieved by targeting some natural amino acid side chains, this often leads to ill-defined and randomly modified proteins. Amongst the natural amino acids, cysteine combines advantageous properties contributing to its suitability for site-selective modification, including a unique nucleophilicity, and a low natural abundance--both allowing chemo- and regioselectivity. Native cysteine residues can be targeted, or Cys can be introduced at a desired site in a protein by means of reliable genetic engineering techniques. This review on chemical protein modification through cysteine should appeal to those interested in modifying proteins for a range of applications.

show abstract

Chemoselective protection of thiols versus alcohols and phenols. The Tosvinyl group

Cited by 28 publications

References 10 publications

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

Bioconjugation with Maleimides: A Useful Tool for Chemical Biology

Chemical Protein Modification through Cysteine

Contact Info

Product

Resources

About