Racemization in the synthesis of polytripeptide models of collagen
Racemization in the synthesis of tripeptide intermediates and their polymers was investigated, using L‐amino acid oxidase. Stepwise investigation of peptide intermediates showed no racemization during peptide coupling steps or deprotection of benzyl esters by hydrogenolysis. Saponification of one of...
Gespeichert in:
| Veröffentlicht in: | Biopolymers 1976-02, Vol.15 (2), p.317-324 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 324 |
|---|---|
| container_issue | 2 |
| container_start_page | 317 |
| container_title | Biopolymers |
| container_volume | 15 |
| creator | Rapaka, Rao S. Bhatnagar, R. S. Nitecki, D. E. |
| description | Racemization in the synthesis of tripeptide intermediates and their polymers was investigated, using L‐amino acid oxidase. Stepwise investigation of peptide intermediates showed no racemization during peptide coupling steps or deprotection of benzyl esters by hydrogenolysis. Saponification of one of the methyl esters produced some racemization. Preparation of active esters from N‐protected tripeptide acids containing optically active C‐terminal amino acid, with one exception, produced racemization. The fractionated polymers were found to contain less racemized amino acids than the crude products or starting monomeric tripeptides, indicating that the racemized sequences gave rise to lower molecular‐weight oligomers. The sequences investigated were ‐Pro‐Pro‐Ala‐, ‐Ala‐Pro‐Pro‐, ‐Val‐Pro‐Pro‐, ‐Pro‐Pro‐Leu‐, ‐Pro‐Gly‐Leu‐, ‐Pro‐Gly‐Phe‐, ‐Pro‐Gly‐Val‐, ‐Gly‐Val‐Pro‐, ‐Phe‐Pro‐Gly‐, ‐Leu‐Pro‐Gly‐, and Ile‐Pro‐Gly‐. |
| doi_str_mv | 10.1002/bip.1976.360150209 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83255419</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>83255419</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3899-81ae1856184285d6c082c425e24f94be052463d2eacf640911b5621cb6d7fdb13</originalsourceid><addsrcrecordid>eNqNkMtO3EAQRVsRiAxDfiBSJK_YeVLVL7slNjBKBiQEIwQku5bdLicd_MLtUTJ8fQxGwJJVLe49V6XD2GeEBQLwr7nvFmgSvRAaUAEH84HNEEwSA0_5DpsBgI6F4uoj2w_hD4CUAmGP7SGXiVZmxk6uMke1f8gG3zaRb6LhN0Vh24wn-BC1ZdS11XbofUfd4AuK6rag6ilwbVVlv6g5YLtlVgX69Hzn7Ob7t-vlaXx-uTpbHp_HTqTGxClmhKnSmEqeqkI7SLmTXBGXpZE5geJSi4JT5kotwSDmSnN0uS6SsshRzNnhtNv17f2GwmBrHxyNTzTUboJNBVdKohmLfCq6vg2hp9J2va-zfmsR7KM4O4qzj-Lsi7gR-vK8vslrKl6RydSYH035X1_R9h2L9uRs_XY-nnAfBvr3gmf9ndWJSJT9cbGysFr_vF0v0WrxH4B5iW8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83255419</pqid></control><display><type>article</type><title>Racemization in the synthesis of polytripeptide models of collagen</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Rapaka, Rao S. ; Bhatnagar, R. S. ; Nitecki, D. E.</creator><creatorcontrib>Rapaka, Rao S. ; Bhatnagar, R. S. ; Nitecki, D. E.</creatorcontrib><description>Racemization in the synthesis of tripeptide intermediates and their polymers was investigated, using L‐amino acid oxidase. Stepwise investigation of peptide intermediates showed no racemization during peptide coupling steps or deprotection of benzyl esters by hydrogenolysis. Saponification of one of the methyl esters produced some racemization. Preparation of active esters from N‐protected tripeptide acids containing optically active C‐terminal amino acid, with one exception, produced racemization. The fractionated polymers were found to contain less racemized amino acids than the crude products or starting monomeric tripeptides, indicating that the racemized sequences gave rise to lower molecular‐weight oligomers. The sequences investigated were ‐Pro‐Pro‐Ala‐, ‐Ala‐Pro‐Pro‐, ‐Val‐Pro‐Pro‐, ‐Pro‐Pro‐Leu‐, ‐Pro‐Gly‐Leu‐, ‐Pro‐Gly‐Phe‐, ‐Pro‐Gly‐Val‐, ‐Gly‐Val‐Pro‐, ‐Phe‐Pro‐Gly‐, ‐Leu‐Pro‐Gly‐, and Ile‐Pro‐Gly‐.</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.1976.360150209</identifier><identifier>PMID: 1247659</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amino Acid Oxidoreductases ; Amino Acid Sequence ; Collagen ; Models, Chemical ; Molecular Weight ; Peptides - chemical synthesis ; Stereoisomerism</subject><ispartof>Biopolymers, 1976-02, Vol.15 (2), p.317-324</ispartof><rights>Copyright © 1976 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3899-81ae1856184285d6c082c425e24f94be052463d2eacf640911b5621cb6d7fdb13</citedby><cites>FETCH-LOGICAL-c3899-81ae1856184285d6c082c425e24f94be052463d2eacf640911b5621cb6d7fdb13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.1976.360150209$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.1976.360150209$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1247659$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rapaka, Rao S.</creatorcontrib><creatorcontrib>Bhatnagar, R. S.</creatorcontrib><creatorcontrib>Nitecki, D. E.</creatorcontrib><title>Racemization in the synthesis of polytripeptide models of collagen</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>Racemization in the synthesis of tripeptide intermediates and their polymers was investigated, using L‐amino acid oxidase. Stepwise investigation of peptide intermediates showed no racemization during peptide coupling steps or deprotection of benzyl esters by hydrogenolysis. Saponification of one of the methyl esters produced some racemization. Preparation of active esters from N‐protected tripeptide acids containing optically active C‐terminal amino acid, with one exception, produced racemization. The fractionated polymers were found to contain less racemized amino acids than the crude products or starting monomeric tripeptides, indicating that the racemized sequences gave rise to lower molecular‐weight oligomers. The sequences investigated were ‐Pro‐Pro‐Ala‐, ‐Ala‐Pro‐Pro‐, ‐Val‐Pro‐Pro‐, ‐Pro‐Pro‐Leu‐, ‐Pro‐Gly‐Leu‐, ‐Pro‐Gly‐Phe‐, ‐Pro‐Gly‐Val‐, ‐Gly‐Val‐Pro‐, ‐Phe‐Pro‐Gly‐, ‐Leu‐Pro‐Gly‐, and Ile‐Pro‐Gly‐.</description><subject>Amino Acid Oxidoreductases</subject><subject>Amino Acid Sequence</subject><subject>Collagen</subject><subject>Models, Chemical</subject><subject>Molecular Weight</subject><subject>Peptides - chemical synthesis</subject><subject>Stereoisomerism</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtO3EAQRVsRiAxDfiBSJK_YeVLVL7slNjBKBiQEIwQku5bdLicd_MLtUTJ8fQxGwJJVLe49V6XD2GeEBQLwr7nvFmgSvRAaUAEH84HNEEwSA0_5DpsBgI6F4uoj2w_hD4CUAmGP7SGXiVZmxk6uMke1f8gG3zaRb6LhN0Vh24wn-BC1ZdS11XbofUfd4AuK6rag6ilwbVVlv6g5YLtlVgX69Hzn7Ob7t-vlaXx-uTpbHp_HTqTGxClmhKnSmEqeqkI7SLmTXBGXpZE5geJSi4JT5kotwSDmSnN0uS6SsshRzNnhtNv17f2GwmBrHxyNTzTUboJNBVdKohmLfCq6vg2hp9J2va-zfmsR7KM4O4qzj-Lsi7gR-vK8vslrKl6RydSYH035X1_R9h2L9uRs_XY-nnAfBvr3gmf9ndWJSJT9cbGysFr_vF0v0WrxH4B5iW8</recordid><startdate>197602</startdate><enddate>197602</enddate><creator>Rapaka, Rao S.</creator><creator>Bhatnagar, R. S.</creator><creator>Nitecki, D. E.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><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>197602</creationdate><title>Racemization in the synthesis of polytripeptide models of collagen</title><author>Rapaka, Rao S. ; Bhatnagar, R. S. ; Nitecki, D. E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3899-81ae1856184285d6c082c425e24f94be052463d2eacf640911b5621cb6d7fdb13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Amino Acid Oxidoreductases</topic><topic>Amino Acid Sequence</topic><topic>Collagen</topic><topic>Models, Chemical</topic><topic>Molecular Weight</topic><topic>Peptides - chemical synthesis</topic><topic>Stereoisomerism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rapaka, Rao S.</creatorcontrib><creatorcontrib>Bhatnagar, R. S.</creatorcontrib><creatorcontrib>Nitecki, D. E.</creatorcontrib><collection>Istex</collection><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>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rapaka, Rao S.</au><au>Bhatnagar, R. S.</au><au>Nitecki, D. E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Racemization in the synthesis of polytripeptide models of collagen</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>1976-02</date><risdate>1976</risdate><volume>15</volume><issue>2</issue><spage>317</spage><epage>324</epage><pages>317-324</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>Racemization in the synthesis of tripeptide intermediates and their polymers was investigated, using L‐amino acid oxidase. Stepwise investigation of peptide intermediates showed no racemization during peptide coupling steps or deprotection of benzyl esters by hydrogenolysis. Saponification of one of the methyl esters produced some racemization. Preparation of active esters from N‐protected tripeptide acids containing optically active C‐terminal amino acid, with one exception, produced racemization. The fractionated polymers were found to contain less racemized amino acids than the crude products or starting monomeric tripeptides, indicating that the racemized sequences gave rise to lower molecular‐weight oligomers. The sequences investigated were ‐Pro‐Pro‐Ala‐, ‐Ala‐Pro‐Pro‐, ‐Val‐Pro‐Pro‐, ‐Pro‐Pro‐Leu‐, ‐Pro‐Gly‐Leu‐, ‐Pro‐Gly‐Phe‐, ‐Pro‐Gly‐Val‐, ‐Gly‐Val‐Pro‐, ‐Phe‐Pro‐Gly‐, ‐Leu‐Pro‐Gly‐, and Ile‐Pro‐Gly‐.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>1247659</pmid><doi>10.1002/bip.1976.360150209</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3525 |
| ispartof | Biopolymers, 1976-02, Vol.15 (2), p.317-324 |
| issn | 0006-3525 1097-0282 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_83255419 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amino Acid Oxidoreductases Amino Acid Sequence Collagen Models, Chemical Molecular Weight Peptides - chemical synthesis Stereoisomerism |
| title | Racemization in the synthesis of polytripeptide models of collagen |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T01%3A37%3A17IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Racemization%20in%20the%20synthesis%20of%20polytripeptide%20models%20of%20collagen&rft.jtitle=Biopolymers&rft.au=Rapaka,%20Rao%20S.&rft.date=1976-02&rft.volume=15&rft.issue=2&rft.spage=317&rft.epage=324&rft.pages=317-324&rft.issn=0006-3525&rft.eissn=1097-0282&rft_id=info:doi/10.1002/bip.1976.360150209&rft_dat=%3Cproquest_cross%3E83255419%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=83255419&rft_id=info:pmid/1247659&rfr_iscdi=true |