Allenamides as Orthogonal Handles for Selective Modification of Cysteine in Peptides and Proteins
Abstract
In this study, a remarkably simple and direct strategy has been successfully developed to selectively label target cysteine residues in fully unprotected peptides and proteins. The strategy is based on the reaction between allenamides and the cysteine thiol, and proceeds swiftly in aqueous medium with excellent selectivity and quantitative conversion, thus forming a stable and irreversible conjugate. The combined simplicity and mildness of the process project allenamide as robust and versatile handles to target cysteines and has potential use in biological systems. Additionally, fluorescent‐labeling studies demonstrated that the installation of a C‐terminal allenamide moiety onto various molecules of interest may supply a new methodology towards the site‐specific labeling of cysteine‐containing proteins. Such a new labeling strategy may thus open a window for its application in the field of life sciences.
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The BAPTES terminal allene carboxamide functional group possesses high chemoselectivity toward the thiol side chain of Cys and forms a stable, irreversible conjugate not prone to hydrolysis.
“The terminal allene carboxamide functional group of the BAPTES ligand possesses high chemoselectivity toward the thiol side chain of Cys, and forms a stable and irreversible conjugate not prone to hydrolysis36.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [36]
Cites
Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology
Chalker, J. M., Bernardes, G. J. L., Lin, Y. A., & Davis, B. G. (2009) · Chemistry - An Asian Journal · doi:10.1002/asia.200800427 · Cited by 653 · see citing works
Protein Modification, Bioconjugation, and Disulfide Bridging Using Bromomaleimides
Smith, M. E. B., Schumacher, F. F., Ryan, C. P., Tedaldi, L. M., Papaioannou, D., Waksman, G., Caddick, S., & Baker, J. R. (2010) · Journal of the American Chemical Society · doi:10.1021/ja908610s · Cited by 378 · see citing works
On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases
Ekkebus, R., van Kasteren, S. I., Kulathu, Y., Scholten, A., Berlin, I., Geurink, P. P., de Jong, A., Goerdayal, S. S., Neefjes, J., Heck, A. J. R., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja309802n · Cited by 346 · see citing works
Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L., & Davis, B. G. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8026168 · Cited by 330 · see citing works
Occurrence, conformational features and amino acid propensities for the π-helix
Fodje, M. N., & Al‐Karadaghi, S. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.5.353 · Cited by 270 · see citing works
Site-Specific PEGylation of Protein Disulfide Bonds Using a Three-Carbon Bridge
Balan, S., Choi, J.-W., Godwin, A., Teo, I. A., Laborde, C. M., Heidelberger, S., Zloh, M., Shaunak, S., & Brocchini, S. (2006) · Bioconjugate Chemistry · doi:10.1021/bc0601471 · Cited by 172 · see citing works
Conjugation-Induced Fluorescent Labeling of Proteins and Polymers Using Dithiomaleimides
Robin, M. P., Wilson, P., Mabire, A. B., Kiviaho, J. K., Raymond, J. E., Haddleton, D. M., & O’Reilly, R. K. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3105494 · Cited by 123 · see citing works
Shiu, H., Chan, T. H., Ho, C., Liu, Y., Wong, M., & Che, C. (2009) · Chemistry - A European Journal · doi:10.1002/chem.200800669 · Cited by 121 · see citing works
Sommer, S., Weikart, N. D., Linne, U., & Mootz, H. D. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.02.039 · Cited by 115 · see citing works
Bromomaleimides: new reagents for the selective and reversible modification of cysteine
Tedaldi, L. M., Smith, M. E. B., Nathani, R. I., & Baker, J. R. (2009) · Chemical Communications · doi:10.1039/b915136b · Cited by 108 · see citing works
Functionalization of Peptides and Proteins by Mukaiyama Aldol Reaction
Alam, J., Keller, T. H., & Loh, T. (2010) · Journal of the American Chemical Society · doi:10.1021/ja102733a · Cited by 67 · see citing works
Self-citationAllylic Selenosulfide Rearrangement: A Method for Chemical Ligation to Cysteine and Other Thiols
Crich, D., Krishnamurthy, V., & Hutton, T. K. (2006) · Journal of the American Chemical Society · doi:10.1021/ja057521c · Cited by 56 · see citing works
Gold-mediated selective cysteine modification of peptides using allenes
Chan, A. O., Tsai, J. L., Lo, V. K., Li, G.-L., Wong, M., & Che, C. (2013) · Chemical Communications · doi:10.1039/c2cc38214h · Cited by 54 · see citing works
The preparation of the first α-vinylidene-β-lactams
Buynak, J. D., Mathew, J., Rao, M. N., Haley, E., George, C., & Siriwardane, U. (1987) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39870000735 · Cited by 33 · see citing works
Arkona, C., & Rademann, J. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303544 · Cited by 25 · see citing works
Roedig, A., & Ritschel, W. (1983) · Chemische Berichte · doi:10.1002/cber.19831160434 · Cited by 14 · see citing works
Arkona, C., & Rademann, J. (2013) · Angewandte Chemie · doi:10.1002/ange.201303544 · Cited by 4 · see citing works
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Sorted by citations
Advances in Chemical Protein Modification
Boutureira, O., & Bernardes, G. J. L. (2015) · Chemical Reviews · doi:10.1021/cr500399p · Cited by 1,137 · see citing works
Click Chemistry in Complex Mixtures: Bioorthogonal Bioconjugation
McKay, C. S., & Finn, M. G. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.002 · Cited by 771 · see citing works
Gehringer, M., & Laufer, S. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01153 · Cited by 757 · see citing works
Residue-Specific Peptide Modification: A Chemist’s Guide
deGruyter, J. N., Malins, L. R., & Baran, P. S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00536 · Cited by 571 · see citing works
Contemporary approaches to site-selective protein modification
Hoyt, E. A., Cal, P. M. S. D., Oliveira, B. L., & Bernardes, G. J. L. (2019) · Nature Reviews Chemistry · doi:10.1038/s41570-019-0079-1 · Cited by 542 · see citing works
Chemical Protein Modification through Cysteine
Gunnoo, S. B., & Madder, A. (2016) · ChemBioChem · doi:10.1002/cbic.201500667 · Cited by 409 · see citing works
Site-Selective C(sp3)–H Functionalization of Di-, Tri-, and Tetrapeptides at the N-Terminus
Gong, W., Zhang, G., Liu, T., Giri, R., & Yu, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510233h · Cited by 290 · see citing works
Covalent Modification of Biomolecules through Maleimide-Based Labeling Strategies
Renault, K., Fredy, J. W., Renard, P., & Sabot, C. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00252 · Cited by 264 · see citing works
Abegg, D., Frei, R., Cerato, L., Hari, D. P., Wang, C., Waser, J., & Adibekian, A. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201505641 · Cited by 158 · see citing works
Kang, M. S., Kong, T. W. S., Khoo, Y. X. J., & Loh, T. (2021) · Chemical Science · doi:10.1039/d1sc02973h · Cited by 151 · see citing works
Self-citationCysteine‐Selective Reactions for Antibody Conjugation
Cal, P. M. S. D., Bernardes, G. J. L., & Góis, P. M. P. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201405702 · Cited by 127 · see citing works
Water-promoted C-S bond formation reactions
Xie, P., Wang, J., Liu, Y., Fan, J., Wo, X., Fu, W., Sun, Z., & Loh, T. (2018) · Nature Communications · doi:10.1038/s41467-018-03698-8 · Cited by 123 · see citing works
Self-citation“Doubly Orthogonal” Labeling of Peptides and Proteins
Tessier, R., Ceballos, J., Guidotti, N., Simonet‐Davin, R., Fierz, B., & Waser, J. (2019) · Chem · doi:10.1016/j.chempr.2019.06.022 · Cited by 118 · see citing works
Field Guide to Challenges and Opportunities in Antibody–Drug Conjugates for Chemists
Gordon, M. R., Canakci, M., Li, L., Zhuang, J., Osborne, B. A., & Thayumanavan, S. (2015) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5b00399 · Cited by 117 · see citing works
Tung, C. L., Wong, C. T. T., Fung, Y. M. E., & Li, X. (2016) · Organic Letters · doi:10.1021/acs.orglett.6b00983 · Cited by 108 · see citing works
Rapid biocompatible macrocyclization of peptides with decafluoro-diphenylsulfone
Kalhor‐Monfared, S., Jafari, M. R., Patterson, J. T., Kitov, P. I., Dwyer, J. J., Nuss, J. M., & Derda, R. (2016) · Chemical Science · doi:10.1039/c5sc03856a · Cited by 104 · see citing works
Recent Progress in Chemical Modification of Proteins
Sakamoto, S., & Hamachi, I. (2018) · Analytical Sciences · doi:10.2116/analsci.18r003 · Cited by 102 · see citing works
Water-soluble allyl sulfones for dual site-specific labelling of proteins and cyclic peptides
Wang, T., Riegger, A., Lamla, M., Wiese, S., Oeckl, P., Otto, M., Wu, Y., Fischer, S., Barth, H., Kuan, S. L., et al. (2016) · Chemical Science · doi:10.1039/c6sc00005c · Cited by 96 · see citing works
Kalia, D., Malekar, P. V., & Parthasarathy, M. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508118 · Cited by 93 · see citing works
Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum
Tiambeng, T. N., Roberts, D. S., Brown, K. A., Zhu, Y., Chen, B., Wu, Z., Mitchell, S. D., Guardado-Alvarez, T. M., Jin, S., & Ge, Y. (2020) · Nature Communications · doi:10.1038/s41467-020-17643-1 · Cited by 76 · see citing works
Kolodych, S., Koniev, O., Baatarkhuu, Z., Bonnefoy, J., Debaene, F., Cianférani, S., DORSSELAER, A. V., & Wagner, A. (2015) · Bioconjugate Chemistry · doi:10.1021/bc500610g · Cited by 73 · see citing works
Chemical technology principles for selective bioconjugation of proteins and antibodies
Chauhan, P. S., Ragendu, V., Kumar, M., Molla, R., Mishra, S. D., Basa, S., & Rai, V. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00715d · Cited by 69 · see citing works
Ariyasu, S., Hayashi, H., Xing, B., & Chiba, S. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00024 · Cited by 67 · see citing works
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Tolnai, G. L., Brand, J. P., & Waser, J. (2016) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.12.74 · Cited by 66 · see citing works
Ahangarpour, M., Kavianinia, I., & Brimble, M. A. (2023) · Organic & Biomolecular Chemistry · doi:10.1039/d2ob02262a · Cited by 55 · see citing works
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Kalia, D., Pawar, S. P., & Thopate, J. S. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201609733 · Cited by 55 · see citing works
A programmable chemical switch based on triggerable Michael acceptors
Zhuang, J., Zhao, B., Meng, X., Schiffman, J. D., Perry, S. L., Vachet, R. W., & Thayumanavan, S. (2020) · Chemical Science · doi:10.1039/c9sc05841a · Cited by 53 · see citing works
Chemical modifications of proteins and their applications in metalloenzyme studies
Naowarojna, N., Cheng, R., Lopez, J., Wong, C., Qiao, L., & Liu, P. (2021) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2021.01.001 · Cited by 52 · see citing works
Selective lysine modification of native peptides via aza-Michael addition
Chen, H., Huang, R., Li, Z., Zhu, W., Chen, J., Zhan, Y., & Jiang, B. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob01866e · Cited by 46 · see citing works
Václavík, J., Zschoche, R., Klimánková, I., Matoušek, V., Beier, P., Hilvert, D., & Togni, A. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201700607 · Cited by 44 · see citing works
Yu, J., Yang, X., Sun, Y., & Yin, Z. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201804801 · Cited by 44 · see citing works
Griffiths, R. C., Smith, F. R., Long, J., Williams, H. E. L., Layfield, R., & Mitchell, N. J. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202006260 · Cited by 44 · see citing works
Synthesis of Vinylic Sulfones in Aqueous Media
Goh, J., Maraswami, M., & Loh, T. (2021) · Organic Letters · doi:10.1021/acs.orglett.0c04257 · Cited by 43 · see citing works
Self-citationAbegg, D., Frei, R., Cerato, L., Hari, D. P., Wang, C., Waser, J., & Adibekian, A. (2015) · Angewandte Chemie · doi:10.1002/ange.201505641 · Cited by 40 · see citing works
Deng, J., Chung, S., Leung, A. S., Yip, W.-M., Yang, B., Choi, M.-C., Cui, J., Kung, K. K., Zhang, Z., Lo, K.-W., et al. (2019) · Communications Chemistry · doi:10.1038/s42004-019-0193-5 · Cited by 38 · see citing works
Silicon-Containing Thiol-Specific Bioconjugating Reagent
Zhang, Z., Li, L., Xu, H., Lee, C.-L. K., Jia, Z., & Loh, T. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12050 · Cited by 37 · see citing works
Self-citationZheng, Y. T., & Song, W. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b00987 · Cited by 36 · see citing works
Chen, Y., Yang, W., Wu, J., Sun, W., Loh, T., & Jiang, Y. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c00415 · Cited by 36 · see citing works
Self-citationCleavable and tunable cysteine-specific arylation modification with aryl thioethers
Li, J., Deng, J., Yin, Z., Hu, Q.-L., Yang, G., Song, Z., Zhang, Y., Chan, A. S. C., Li, H., & Xiong, X. (2021) · Chemical Science · doi:10.1039/d0sc06576e · Cited by 35 · see citing works
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Hou, Z., Wang, D., Li, Y., Zhao, R., Wan, C., Ma, Y., Lian, C., Yin, F., & Li, Z. (2020) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.9b02505 · Cited by 34 · see citing works
Recent advances in protein modifications techniques for the targeting N‐terminal cysteine
Asiimwe, N., Mazid, M. F. A., Murale, D. P., Kim, Y. K., & Lee, J. (2021) · Peptide Science · doi:10.1002/pep2.24235 · Cited by 34 · see citing works
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Bi, X., Yin, J., Guanbang, A. C., & Liu, C. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201705049 · Cited by 34 · see citing works
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Cal, P. M. S. D., Bernardes, G. J. L., & Góis, P. M. P. (2014) · Angewandte Chemie · doi:10.1002/ange.201405702 · Cited by 33 · see citing works
Assessment of reagents for selenocysteine conjugation and the stability of selenocysteine adducts
Pedzisa, L., Li, X., Rader, C. M., & Roush, W. R. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00775a · Cited by 33 · see citing works
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Chen, D., Guo, D., Yan, Z., & Zhao, Y. (2017) · MedChemComm · doi:10.1039/c7md00571g · Cited by 32 · see citing works
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Fung, E., Chua, K. J., Ganz, T., Nemeth, E., & Ruchala, P. P. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.12.094 · Cited by 31 · see citing works
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Tang, K. C., Maddox, S. M., Backus, K. M., & Raj, M. (2021) · Chemical Science · doi:10.1039/d1sc04139h · Cited by 31 · see citing works
Cameron, A. J., Harris, P. W. R., & Brimble, M. A. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004656 · Cited by 30 · see citing works
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Lu, M., & Loh, T. (2023) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00555 · Cited by 28 · see citing works
Self-citationKang, M. S., Khoo, Y. X. J., Jia, Z., & Loh, T. (2022) · Green Synthesis and Catalysis · doi:10.1016/j.gresc.2022.09.002 · Cited by 28 · see citing works
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Wang, C., Zhao, Z., Ghadir, R., Yang, D., Zhang, Z., Ding, Z., Cao, Y., Li, Y., Fassler, R., Reichmann, D., et al. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c01148 · Cited by 26 · see citing works
Song, L., Tian, G., Blanpain, A., Meervelt, L. V., & der Eycken, E. V. V. (2019) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201900550 · Cited by 25 · see citing works
Mishra, D. R., Panda, B. S., Nayak, S., Panda, J., & Mohapatra, S. (2022) · ChemistrySelect · doi:10.1002/slct.202200531 · Cited by 24 · see citing works
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Huang, R., Li, Z., Sheng, Y., Yu, J., Wu, Y., Zhan, Y., Chen, H., & Jiang, B. (2018) · Organic Letters · doi:10.1021/acs.orglett.8b02849 · Cited by 24 · see citing works
Zheng, Y. T., Song, W., Zhu, Y., Wei, B., & Xuan, L. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00207j · Cited by 23 · see citing works
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Teng, S., Ng, E. W. H., Zhang, Z., Soon, C. N., Xu, H., Li, R., Hirao, H., & Loh, T. (2023) · Science Advances · doi:10.1126/sciadv.adg4924 · Cited by 22 · see citing works
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Self-citationCosta, A. M., Bosch, L., Petit, E., & Vilarrasa, J. (2021) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.1c00349 · Cited by 21 · see citing works
Bahou, C., Szijj, P. A., Spears, R. J., Wall, A., Javaid, F., Sattikar, A., Love, E. A., Baker, J. R., & Chudasama, V. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00057 · Cited by 21 · see citing works
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Tang, J. S., Lu, F., Geng, Y., Liu, Y., & Zhang, E. (2023) · Organic Letters · doi:10.1021/acs.orglett.3c01952 · Cited by 18 · see citing works
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Goh, J., Ong, S. K., Tan, Y. S., & Loh, T. (2022) · Green Chemistry · doi:10.1039/d2gc00027j · Cited by 16 · see citing works
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Wynne, C., & Elmes, R. B. P. (2024) · Sensors & Diagnostics · doi:10.1039/d4sd00022f · Cited by 16 · see citing works
Xiang, F., Hu, F., Weng, Y., & Gao, M. (2024) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202400772 · Cited by 16 · see citing works
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Self-citationKalia, D., Malekar, P. V., & Parthasarathy, M. (2015) · Angewandte Chemie · doi:10.1002/ange.201508118 · Cited by 14 · see citing works
Bao, C., & Zhang, Q. (2019) · European Polymer Journal · doi:10.1016/j.eurpolymj.2019.01.020 · Cited by 13 · see citing works
Silva, M. J., Cavadas, R. A. N., Faustino, H., Veiros, L. F., & Góis, P. M. P. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202202377 · Cited by 13 · see citing works
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Wang, C., Zhao, Y., & Zhao, J. (2022) · Chinese Journal of Organic Chemistry · doi:10.6023/cjoc202203008 · Cited by 13 · see citing works
Na, T., Sander, V., Davidson, A. J., Lin, R., Hermant, Y. O., Boys, M. T. H., Pletzer, D., Campbell, G., Ferguson, S. A., Cook, G. M., et al. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202407764 · Cited by 12 · see citing works
Jo, H., Ju, S., Kim, M., Beon, J., Jang, S.-Y., Pack, S. P., Son, C. Y., Kim, J., & Oh, S. S. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c15674 · Cited by 12 · see citing works
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Veltri, L., Amuso, R., Vitale, P., Chiacchio, M. A., Benincasa, C., & Gabriele, B. (2021) · Journal of CO2 Utilization · doi:10.1016/j.jcou.2021.101695 · Cited by 11 · see citing works
Tao, X., Ma, G., Song, Y., Chen, Y., Qian, Q., Sun, D., & Gong, H. (2021) · Organic Letters · doi:10.1021/acs.orglett.1c02601 · Cited by 11 · see citing works
Yu, J., Yang, X., Sun, Y., & Yin, Z. (2018) · Angewandte Chemie · doi:10.1002/ange.201804801 · Cited by 11 · see citing works
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Brun, O., Agramunt, J., Raich, L., Rovira, C., Pedroso, E., & Grandas, A. (2016) · Organic Letters · doi:10.1021/acs.orglett.6b02301 · Cited by 10 · see citing works
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Deng, M.-L., Sheng, M.-W., Wen, X.-K., Cao, R.-N., Li, M., Loh, T., & Lu, M. (2025) · Organic Letters · doi:10.1021/acs.orglett.5c01110 · Cited by 9 · see citing works
Self-citationLiu, Q., Li, Z., Huang, Y., Lin, Z., Shen, X., & Chen, H. (2025) · Chemical Science · doi:10.1039/d5sc06690e · Cited by 9 · see citing works
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Kalia, D., Pawar, S. P., & Thopate, J. S. (2017) · Angewandte Chemie · doi:10.1002/ange.201609733 · Cited by 8 · see citing works
Tasdan, Y., Balaji, G. R., Akhtar, N., Ilyichova, O. V., Cunliffe, T., Heras, B., Strat, L. L., Murray, J. B., Capuano, B., Scanlon, M. J., et al. (2025) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00016 · Cited by 7 · see citing works
Wang, L., Mondal, B., Li, B., Zhang, Z., Loh, T., Chen, P., & Jia, Z. (2025) · ACS Catalysis · doi:10.1021/acscatal.5c06339 · Cited by 7 · see citing works
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Gavriel, K., & Neumann, K. (2026) · Precision Chemistry · doi:10.1021/prechem.5c00323 · Cited by 7 · see citing works
Wa‐Yi, O., Cui, J., Yu, Q., Kung, K. K., Chung, S., Leung, Y., & Wong, M. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202218038 · Cited by 7 · see citing works
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Brulet, J. W., Ciancone, A. M., Yuan, K., & Hsu, K. (2023) · Israel Journal of Chemistry · doi:10.1002/ijch.202300001 · Cited by 6 · see citing works
Shepperson, O. A., Harris, P. W. R., Brimble, M. A., & Cameron, A. J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1487338 · Cited by 6 · see citing works
Sreejith, S., Kishor, R., Abbas, A., Thomas, R., Yeo, T., Ranjan, V., Vaidyanathan, R., Seah, Y. P., Xing, B., Wang, Z., et al. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b20315 · Cited by 6 · see citing works
Self-citationShepperson, O. A., Harris, P. W. R., Brimble, M. A., & Cameron, A. J. (2024) · Antibiotics · doi:10.3390/antibiotics13070615 · Cited by 5 · see citing works
Kiattisewee, C., Kaidad, A., Jiarpinitnun, C., & Luanphaisarnnont, T. (2018) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-018-2175-1 · Cited by 5 · see citing works
Cameron, A. J., Harris, P. W. R., & Brimble, M. A. (2020) · Angewandte Chemie · doi:10.1002/ange.202004656 · Cited by 5 · see citing works
Catalyst-Free Reactions under Biocompatible Conditions
Loh, T., Ren, M., & Lu, M. (2022) · Synlett · doi:10.1055/a-1994-3327 · Cited by 5 · see citing works
Self-citationTracking down protein–protein interactions via a FRET-system using site-specific thiol-labeling
Söveges, B., Imre, T., Póti, Á., Sok, P., Kele, Z., Alexa, A., Kele, P., & Németh, K. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00742j · Cited by 5 · see citing works
Griffiths, R. C., Smith, F. R., Long, J., Williams, H. E. L., Layfield, R., & Mitchell, N. J. (2020) · Angewandte Chemie · doi:10.1002/ange.202006260 · Cited by 6 · see citing works
Biocompatible ultrafast thiol-acetalization enabled by triaryl carbenium ion-pair
Chen, P., Zou, M., Zhang, Y., Li, N., Ruiding, L. I., Liang, L., Zhang, Z., Loh, T., & Jia, Z. (2025) · Green Chemistry · doi:10.1039/d5gc03823e · Cited by 5 · see citing works
Self-citationComputational study on the mechanism of CBT-Cys click reaction
Xu, Y., Qi, C., & Wang, C. (2020) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2020.112874 · Cited by 4 · see citing works
Shvetsov, A. B., & Semenov, A. (2024) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162024060347 · Cited by 3 · see citing works
Zhang, Z., Ji, M.-M., Wu, X., He, Y.-Y., & Peng, J. (2024) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.4c00977 · Cited by 3 · see citing works
1,2-Allenic Ketone-Based Fluorogenic Probes for Imaging of S-Sulfinylation in Living Cells
Wu, L., Liu, K., Shi, Y., Peng, Y., Wang, J., Zhang, C., Strongin, R. M., & Yang, X. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.4c05887 · Cited by 3 · see citing works
- Authors
- Abbas, A., Xing, B., & Loh, T.
- Affiliations
- Nanyang Technological University (SG)
- University of Science and Technology of China (CN)
- Corresponding author
- Xing, Bengang
- Loh, Teck‐Peng
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2014-05-30
- Volume
- 53
- Issue
- 29
- Pages
- 7491-7494
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W4234076445
- Cited by
- 117
- References
- 17
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 12 · 2023: 11 · 2022: 6 · 2021: 11 · 2020: 11 · 2019: 8 · 2018: 12 · 2017: 7 · 2016: 8 · 2015: 9 · 2014: 4
- FWCI
- 4.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Angewandte Chemie International Edition (publishedVersion)
- PubMed (publishedVersion)
- DR-NTU (Nanyang Technological University) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Physical Sciences › Chemistry › Organic Chemistry › Sulfur-Based Synthesis Techniques
- Keywords
- allenamides, cysteine labeling, site-specific protein modification, thiol-ene reaction, peptide modification, fluorescent labeling, cysteine-containing proteins
- MeSH terms
- Amides, Cysteine, Fluorescent Dyes, Peptides, Proteins
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