Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine
[Display omitted] Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2017-09, Vol.25 (18), p.4983-4989 |
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| container_title | Bioorganic & medicinal chemistry |
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| creator | Dardashti, Rebecca Notis Metanis, Norman |
| description | [Display omitted]
Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols. |
| doi_str_mv | 10.1016/j.bmc.2017.05.006 |
| format | Article |
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Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols.</description><identifier>ISSN: 0968-0896</identifier><identifier>EISSN: 1464-3391</identifier><identifier>DOI: 10.1016/j.bmc.2017.05.006</identifier><identifier>PMID: 28526476</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Chalcogens - chemistry ; Chemical protein synthesis ; Chromatography, High Pressure Liquid ; Methylation ; Native chemical ligation ; Peptide methylation ; Peptides - analysis ; Peptides - chemical synthesis ; Peptides - chemistry ; Selenocysteine ; Selenocysteine - analogs & derivatives ; Selenocysteine - chemistry ; Selenomethionine ; Selenomethionine - chemistry</subject><ispartof>Bioorganic & medicinal chemistry, 2017-09, Vol.25 (18), p.4983-4989</ispartof><rights>2017 Elsevier Ltd</rights><rights>Copyright © 2017 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-c5112b51f3d66ee723922fa53a3fd2b1d8f4ec05b7b2376951331816742410043</citedby><cites>FETCH-LOGICAL-c353t-c5112b51f3d66ee723922fa53a3fd2b1d8f4ec05b7b2376951331816742410043</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0968089617306831$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28526476$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dardashti, Rebecca Notis</creatorcontrib><creatorcontrib>Metanis, Norman</creatorcontrib><title>Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>[Display omitted]
Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols.</description><subject>Amino Acid Sequence</subject><subject>Chalcogens - chemistry</subject><subject>Chemical protein synthesis</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Methylation</subject><subject>Native chemical ligation</subject><subject>Peptide methylation</subject><subject>Peptides - analysis</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Selenocysteine</subject><subject>Selenocysteine - analogs & derivatives</subject><subject>Selenocysteine - chemistry</subject><subject>Selenomethionine</subject><subject>Selenomethionine - chemistry</subject><issn>0968-0896</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kFFrFDEUhYNY7Fr9Ab5IHn2Z8d5kkpnRJymtFgoF0eeQydzZzTKT1El2sf_elK2CID5dOHznwP0Ye4NQI6B-v6-HxdUCsK1B1QD6Gdtgo5tKyh6fsw30uqug6_U5e5nSHgBE0-MLdi46JXTT6g37-ZWOPvnsw5bPfmuzj4HbzBPNFOJCeVcCH-gDvwnJb3c5cR9y5KGQR-JuR4t3dv5H1z2kTKXJbRj5Li7x7_gVO5vsnOj1071g36-vvl1-qW7vPt9cfrqtnFQyV04hikHhJEetiVoheyEmq6SV0ygGHLupIQdqaAchW90rlBI71G0jGgRo5AV7d9q9X-OPA6VsFp8czbMNFA_JYA_QSSGhLyieULfGlFaazP3qF7s-GATzKNzsTRFuHoUbUKYIL523T_OHYaHxT-O34QJ8PAFUnjx6Wk1ynoKj0a_kshmj_8_8LztTkrI</recordid><startdate>20170915</startdate><enddate>20170915</enddate><creator>Dardashti, Rebecca Notis</creator><creator>Metanis, Norman</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20170915</creationdate><title>Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine</title><author>Dardashti, Rebecca Notis ; Metanis, Norman</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-c5112b51f3d66ee723922fa53a3fd2b1d8f4ec05b7b2376951331816742410043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Sequence</topic><topic>Chalcogens - chemistry</topic><topic>Chemical protein synthesis</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Methylation</topic><topic>Native chemical ligation</topic><topic>Peptide methylation</topic><topic>Peptides - analysis</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Selenocysteine</topic><topic>Selenocysteine - analogs & derivatives</topic><topic>Selenocysteine - chemistry</topic><topic>Selenomethionine</topic><topic>Selenomethionine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dardashti, Rebecca Notis</creatorcontrib><creatorcontrib>Metanis, Norman</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dardashti, Rebecca Notis</au><au>Metanis, Norman</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>2017-09-15</date><risdate>2017</risdate><volume>25</volume><issue>18</issue><spage>4983</spage><epage>4989</epage><pages>4983-4989</pages><issn>0968-0896</issn><eissn>1464-3391</eissn><abstract>[Display omitted]
Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>28526476</pmid><doi>10.1016/j.bmc.2017.05.006</doi><tpages>7</tpages></addata></record> |
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| ispartof | Bioorganic & medicinal chemistry, 2017-09, Vol.25 (18), p.4983-4989 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Chalcogens - chemistry Chemical protein synthesis Chromatography, High Pressure Liquid Methylation Native chemical ligation Peptide methylation Peptides - analysis Peptides - chemical synthesis Peptides - chemistry Selenocysteine Selenocysteine - analogs & derivatives Selenocysteine - chemistry Selenomethionine Selenomethionine - chemistry |
| title | Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine |
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