4卷 第2期
Some Methods about Protein Cyclisation
Some Methods about Protein Cyclisation
- 2023年4卷第2期 页码:18-23
纸质出版日期: 2023
DOI:10.47297/taposatWSP2633-456903.20230402
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4卷 第2期
West China School of Pharmacy, Sichuan University, Chendu Sichuan,P.R. China,610065
纸质出版日期: 2023 ,
Scan QR Code
(2023). Some Methods about Protein Cyclisation. 科技理论与实践(英文版), 4(2), 18-23.
Lezhi Wang. (2023). Some Methods about Protein Cyclisation. Theory and Practice of Science and Technology, 4(2), 18-23.
(2023). Some Methods about Protein Cyclisation. 科技理论与实践(英文版), 4(2), 18-23. DOI: 10.47297/taposatWSP2633-456903.20230402.
Lezhi Wang. (2023). Some Methods about Protein Cyclisation. Theory and Practice of Science and Technology, 4(2), 18-23. DOI: 10.47297/taposatWSP2633-456903.20230402.
Proteins are crucial to exerting biological functions
while they are stable under some specific circumstances limiting their widely use in various fields. One approach called protein cyclisation
especially cyclised polypeptides which are proved to be beneficial to the stability of proteins both in laboratory and nature world
they are expected to have a widely use in many fields including food
health care and pharmaceutical industries. So it is of great importance to develop approaches to achieve the cyclisation of protein and peptides
fortunately
a lot of related researches have been reported over the past few decades. This review illustrates some approaches about protein cyclisation
including chemical methods and enzymatic methods
and some features of each approach and under what conditions it would be the best choice are discussed
advantages and limitations are also discussed in this article.
Protein cyclisationChemical methodsEnzymatic methodsAdvantages and limitations
Aboye, T. L., & Camarero, J. A. (2012). Biological synthesis of circular polypeptides. Journal of Biological Chemistry, 287(32), 27026-27032. [2]Hayes, H. C., Luk, L. Y., & Tsai, Y. H. (2021). Approaches for peptide and protein cyclisation. Organic & biomolecular chemistry, 19(18), 3983-4001.[3]de Araujo, A. D., Nguyen, H. T., & Fairlie, D. P. (2021). Late-Stage Hydrocarbon Conjugation and Cyclisation in Synthetic Peptides and Proteins. ChemBioChem, 22(10), 1784-89.[4]Martin, N., & Cirujano, F. G. (2022). Heterogeneous catalytic direct amide bond formation. Catalysis Communications, 164, 106420.[5]Perreux, L., Loupy, A., & Volatron, F. (2002). Solvent-free preparation of amides from acids and primary amines under microwave irradiation. Tetrahedron, 58(11), 2155-62.[6]Sabatini, M. T., Boulton, L. T., Sneddon, H. F., & Sheppard, T. D. (2019). A green chemistry perspective on catalytic amide bond formation. Nature Catalysis, 2(1), 10-17.[7]Valeur, E., & Bradley, M. (2009). Amide bond formation: beyond the myth of coupling reagents. Chemical Society Reviews, 38(2), 606-31.[8]Montalbetti, C. A., & Falque, V. (2005). Amide bond formation and peptide coupling. Tetrahedron, 61(46), 10827-10852.[9]Agouridas, V., El Mahdi, O., Diemer, V., Cargoët, M., Monbaliu, J. C. M., & Melnyk, O. (2019). Native chemical ligation and extended methods: mechanisms, catalysis, scope, and limitations. Chemical reviews, 119(12), 7328-7443.[10]Castro, E. A. (2007). Kinetics and mechanisms of reactions of thiol, thiono and dithio analogues of carboxylic esters with nucleophiles. An update. Journal of Sulfur Chemistry, 28(4), 401-29.[11]Adams, A. L., Cowper, B., Morgan, R. E., Premdjee, B., Caddick, S., & Macmillan, D. (2013). Cysteine promoted C-terminal hydrazinolysis of native peptides and proteins. Angewandte Chemie, 125(49), 13300-13304.[12]Li, X., Lam, H. Y., Zhang, Y., & Chan, C. K. (2010). Salicylaldehyde ester-induced chemoselective peptide ligations: enabling generation of natural peptidic linkages at the serine/threonine sites. Organic letters, 12(8), 1724-27.[13]Sletten, E. M., & Bertozzi, C. R. (2011). From mechanism to mouse: a tale of two bioorthogonal reactions. Accounts of chemical research, 44(9), 666-76.[14]Lang, K., & Chin, J. W. (2014). Bioorthogonal reactions for labeling proteins. ACS chemical biology, 9(1), 16-20.[15]Row, R. D., & Prescher, J. A. (2018). Constructing new bioorthogonal reagents and reactions. Accounts of chemical research, 51(5), 1073-1081.[16]Hur, G. H., Vickery, C. R., & Burkart, M. D. (2012). Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology. Natural product reports, 29(10), 1074-98.[17]Mootz, H. D., Schwarzer, D., & Marahiel, M. A. (2002). Ways of assembling complex natural products on modular nonribosomal peptide synthetases. ChemBioChem, 3(6), 490-504.[18]Lee, S. G., & Lipmann, F. (1977). Isolation of amino acid activating subunit-pantetheine protein complexes: Their role in chain elongation in tyrocidine synthesis. Proceedings of the National Academy of Sciences, 74(6), 2343-47.[19]Yokoyama, K., Nio, N., & Kikuchi, Y. (2004). Properties and applications of microbial transglutaminase. Applied microbiology and biotechnology, 64, 447-54.[20]Touati, J., Angelini, A., Hinner, M. J., & Heinis, C. (2011). Enzymatic cyclisation of peptides with a transglutaminase. ChemBioChem, 12(1), 38-42.[21]Hara-Nishimura, I., Takeuchi, Y., & Nishimura, M. (1993). Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. The Plant Cell, 5(11), 1651-59.[22]Dall, E., & Brandstetter, H. (2013). Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation. Proceedings of the National Academy of Sciences, 110(27), 10940-10945.[23]Tang, T. S., & Luk, L. Y. (2021). Asparaginyl endopeptidases: enzymology, applications and limitations. Organic & Biomolecular Chemistry, 19(23), 5048-62.
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