Genetically encoded alkenyl–pyrrolysine analogues for thiol–ene reaction mediated site-specific protein labeling

Li, Yiming; Yang, Mao; Huang, Yichao; Song, Xiaoda; Liu, Lei; Chen, Peng R.

doi:10.1039/c2sc20433a

Cited by 50 publications

(45 citation statements)

References 80 publications

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“…Oxidative elimination by treatment with O-mesitylenesulfonyl hydroxylamine (MSH) under basic conditions affords dehydroalanine (Bernardes et al, 2008), which can be modified by conjugate addition of thiols (entry 17) (Chalker et al, 2009a), or can undergo olefin cross-metathesis with ruthenium catalysts (Lin et al, 2008). Additionally, thiol-ene click reactions that are so useful in materials contexts have also been used for bioconjugation (entry 18), as in the glycosylation of a single cysteine moiety on glutathione (Dondoni et al, 2009) or the labeling of alkyne-bearing proteins expressed in E. coli (Li et al, 2013b; Li et al, 2012). …”

Section: B Bioorthogonal Conjugation Strategies and Applicationsmentioning

confidence: 99%

Click Chemistry in Complex Mixtures: Bioorthogonal Bioconjugation

McKay

Finn

2014

Chemistry & Biology

670

555

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The selective chemical modification of biological molecules drives a good portion of modern drug development and fundamental biological research. While a few early examples of reactions that engage amine and thiol groups on proteins helped establish the value of such processes, the development of reactions that avoid most biological molecules so as to achieve selectivity in desired bond-forming events has revolutionized the field. We provide an update on recent developments in bioorthogonal chemistry that highlights key advances in reaction rates, biocompatibility, and applications. While not exhaustive, we hope this summary allows the reader to appreciate the rich continuing development of good chemistry that operates in the biological setting.

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Section: B Bioorthogonal Conjugation Strategies and Applicationsmentioning

confidence: 99%

Click Chemistry in Complex Mixtures: Bioorthogonal Bioconjugation

McKay

Finn

2014

Chemistry & Biology

670

555

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“…Selective labeling of proteins incorporated with 6 and another terminal alkene-containing PylRS substrate 7 using the thio-ene photoclick reaction has been demonstrated. [66] Kryzcki et al also sought alternative PylRS substrates independently. They discovered that 8 maintained about 9% of the activity of Pyl as a PylRS substrate.…”

Section: An Outstanding Genetic Code Expansion Toolmentioning

confidence: 99%

“…6 – 7 and 24 have a terminal alkene that has been demonstrated to undergo thio-ene photoclick protein labeling. [66] 15–17 can be applied to undergo native chemical ligation for the synthesis of ubiquitinated proteins and a biocompatible condensation for protein labeling. [78–80] 25 and 27 has an azide that selectively undergoes the Staudinger ligation, CuAAC click, and Cu-free click reactions.…”

Section: An Outstanding Genetic Code Expansion Toolmentioning

confidence: 99%

Pyrrolysyl-tRNA synthetase: An ordinary enzyme but an outstanding genetic code expansion tool

Wan¹,

Tharp²,

Liu³

2014

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

363

418

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The genetic incorporation of the 22nd proteinogenic amino acid, pyrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNAPyl. Unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate α-amine, and low selectivity toward the anticodon of tRNAPyl. These unique but ordinary features of PylRS as an aminoacyl-tRNA synthetase allow the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (NCAAs) or α-hydroxy acids into proteins at amber codon and the reassignment of other codons such as ochre UAA, opal UGA, and four-base AGGA codons to code NCAAs.

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“…Wittrock et al 182 first reported the use of the classical radical thiol-ene (thiyl-ene) reaction between thiols and olefins as a method for modifying thiol-containing proteins under ultraviolet irradiation. This has subsequently been exploited at both genetically encoded alkenes 169,183 and native cysteine residues 184 to generate glycoprotein mimics 169,184 , and for surface immobilisation of proteins 172 . A related reaction, the thiol-yne reaction with alkynes, has also been reported 100,185 .…”

Section: Modifications At Uaasmentioning

confidence: 99%