Chemical synthesis of circular proteins
Circular proteins, once thought to be rare, are now commonly found in plants. Their chemical synthesis, once thought to be difficult, is now readily achievable. The enabling methodology is largely due to the advances in entropic chemical ligation to overcome the entropy barrier in coupling the N- an...
| Main Authors: | , |
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| Format: | Journal Article |
| Language: | English |
| Published: |
2013
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| Online Access: | https://hdl.handle.net/10356/103952 http://hdl.handle.net/10220/17091 |
| _version_ | 1826112020202651648 |
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| author | Tam, James P. Wong, Clarence T. T. |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Tam, James P. Wong, Clarence T. T. |
| author_sort | Tam, James P. |
| collection | NTU |
| description | Circular proteins, once thought to be rare, are now commonly found in plants. Their chemical synthesis, once thought to be difficult, is now readily achievable. The enabling methodology is largely due to the advances in entropic chemical ligation to overcome the entropy barrier in coupling the N- and C-terminal ends of large peptide segments for either intermolecular ligation or intramolecular ligation in end-to-end cyclization. Key elements of an entropic chemical ligation consist of a chemoselective capture step merging the N and C termini as a covalently linked O/S-ester intermediate to permit the subsequent step of an intramolecular O/S-N acyl shift to form an amide. Many ligation methods exploit the supernucleophilicity of a thiol side chain at the N terminus for the capture reaction, which makes cysteine-rich peptides ideal candidates for the entropy-driven macrocyclization. Advances in desulfurization and modification of the thiol-containing amino acids at the ligation sites to other amino acids add extra dimensions to the entropy-driven ligation methods. This minireview describes recent advances of entropy-driven ligation to prepare circular proteins with or without a cysteinyl side chain. |
| first_indexed | 2024-10-01T03:00:26Z |
| format | Journal Article |
| id | ntu-10356/103952 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T03:00:26Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/1039522022-02-16T16:28:09Z Chemical synthesis of circular proteins Tam, James P. Wong, Clarence T. T. School of Biological Sciences DRNTU::Science::Biological sciences Circular proteins, once thought to be rare, are now commonly found in plants. Their chemical synthesis, once thought to be difficult, is now readily achievable. The enabling methodology is largely due to the advances in entropic chemical ligation to overcome the entropy barrier in coupling the N- and C-terminal ends of large peptide segments for either intermolecular ligation or intramolecular ligation in end-to-end cyclization. Key elements of an entropic chemical ligation consist of a chemoselective capture step merging the N and C termini as a covalently linked O/S-ester intermediate to permit the subsequent step of an intramolecular O/S-N acyl shift to form an amide. Many ligation methods exploit the supernucleophilicity of a thiol side chain at the N terminus for the capture reaction, which makes cysteine-rich peptides ideal candidates for the entropy-driven macrocyclization. Advances in desulfurization and modification of the thiol-containing amino acids at the ligation sites to other amino acids add extra dimensions to the entropy-driven ligation methods. This minireview describes recent advances of entropy-driven ligation to prepare circular proteins with or without a cysteinyl side chain. 2013-10-31T01:32:06Z 2019-12-06T21:23:30Z 2013-10-31T01:32:06Z 2019-12-06T21:23:30Z 2012 2012 Journal Article Tam, J. P., & Wong, C. T. T. (2012). Chemical synthesis of circular proteins. Journal of biological chemistry, 287(32), 27020-27025. https://hdl.handle.net/10356/103952 http://hdl.handle.net/10220/17091 10.1074/jbc.R111.323568 22700959 en Journal of biological chemistry © 2012 The American Society for Biochemistry and Molecular Biology, Inc. |
| spellingShingle | DRNTU::Science::Biological sciences Tam, James P. Wong, Clarence T. T. Chemical synthesis of circular proteins |
| title | Chemical synthesis of circular proteins |
| title_full | Chemical synthesis of circular proteins |
| title_fullStr | Chemical synthesis of circular proteins |
| title_full_unstemmed | Chemical synthesis of circular proteins |
| title_short | Chemical synthesis of circular proteins |
| title_sort | chemical synthesis of circular proteins |
| topic | DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/103952 http://hdl.handle.net/10220/17091 |
| work_keys_str_mv | AT tamjamesp chemicalsynthesisofcircularproteins AT wongclarencett chemicalsynthesisofcircularproteins |