Total chemical synthesis of human activin βA[12-116] and related large-loop polypeptides
We report here the synthesis, purification, and characterization of several large polypeptides related to the human activin βA subunit and their cyclic counterparts. In particular, we describe for the first time the total chemical synthesis of a 105‐mer polypeptide, des[1–11] activin βA, and related...
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Veröffentlicht in: | Biopolymers 2001, Vol.60 (4), p.279-289 |
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creator | Keah, Hooi Hong Allen, Natalie Clay, Robert Boysen, Reinhard I. Warner, Tracy Hearn, Milton T. W. |
description | We report here the synthesis, purification, and characterization of several large polypeptides related to the human activin βA subunit and their cyclic counterparts. In particular, we describe for the first time the total chemical synthesis of a 105‐mer polypeptide, des[1–11] activin βA, and related large‐loop polypeptide, by an optimized solid phase synthetic protocol based on 9‐flouroenylmethyoxycarbonyl (Fmoc) chemistry. These studies show that automated chemical synthesis utilizing Fmoc‐based solid phase synthetic strategies provides a practical alternative to recombinant DNA technology for the production of activin‐related subunits, with the opportunity to rapidly provide different analogues and structural variants for subsequent structure–function and associated biophysical investigations. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 60: 279–289, 2001 |
doi_str_mv | 10.1002/1097-0282(2001)60:4<279::AID-BIP9990>3.0.CO;2-M |
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W.</creator><creatorcontrib>Keah, Hooi Hong ; Allen, Natalie ; Clay, Robert ; Boysen, Reinhard I. ; Warner, Tracy ; Hearn, Milton T. W.</creatorcontrib><description>We report here the synthesis, purification, and characterization of several large polypeptides related to the human activin βA subunit and their cyclic counterparts. In particular, we describe for the first time the total chemical synthesis of a 105‐mer polypeptide, des[1–11] activin βA, and related large‐loop polypeptide, by an optimized solid phase synthetic protocol based on 9‐flouroenylmethyoxycarbonyl (Fmoc) chemistry. These studies show that automated chemical synthesis utilizing Fmoc‐based solid phase synthetic strategies provides a practical alternative to recombinant DNA technology for the production of activin‐related subunits, with the opportunity to rapidly provide different analogues and structural variants for subsequent structure–function and associated biophysical investigations. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 60: 279–289, 2001</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/1097-0282(2001)60:4<279::AID-BIP9990>3.0.CO;2-M</identifier><identifier>PMID: 11774231</identifier><language>eng</language><publisher>New York: John Wiley & Sons, Inc</publisher><subject>Activins - chemistry ; alpha-Macroglobulins - chemistry ; Amino Acid Sequence ; chemical synthesis ; Chromatography, High Pressure Liquid ; Dose-Response Relationship, Drug ; Electrophoresis, Polyacrylamide Gel ; ESI-MS ; Fluorenes - chemistry ; Fmoc-solid ; human activin βA[12-116] ; Humans ; Inhibin-beta Subunits - chemical synthesis ; Inhibin-beta Subunits - chemistry ; Kinetics ; large-loop polypeptides ; Molecular Sequence Data ; Peptide Biosynthesis ; Peptides - chemical synthesis ; Peptides - chemistry ; phase methods ; Protein Binding ; Protein Conformation ; Time Factors ; Transformation, Genetic</subject><ispartof>Biopolymers, 2001, Vol.60 (4), p.279-289</ispartof><rights>Copyright © 2001 John Wiley & Sons, Inc.</rights><rights>Copyright 2001 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1097-0282%282001%2960%3A4%3C279%3A%3AAID-BIP9990%3E3.0.CO%3B2-M$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1097-0282%282001%2960%3A4%3C279%3A%3AAID-BIP9990%3E3.0.CO%3B2-M$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,4010,27900,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11774231$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Keah, Hooi Hong</creatorcontrib><creatorcontrib>Allen, Natalie</creatorcontrib><creatorcontrib>Clay, Robert</creatorcontrib><creatorcontrib>Boysen, Reinhard I.</creatorcontrib><creatorcontrib>Warner, Tracy</creatorcontrib><creatorcontrib>Hearn, Milton T. W.</creatorcontrib><title>Total chemical synthesis of human activin βA[12-116] and related large-loop polypeptides</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>We report here the synthesis, purification, and characterization of several large polypeptides related to the human activin βA subunit and their cyclic counterparts. In particular, we describe for the first time the total chemical synthesis of a 105‐mer polypeptide, des[1–11] activin βA, and related large‐loop polypeptide, by an optimized solid phase synthetic protocol based on 9‐flouroenylmethyoxycarbonyl (Fmoc) chemistry. These studies show that automated chemical synthesis utilizing Fmoc‐based solid phase synthetic strategies provides a practical alternative to recombinant DNA technology for the production of activin‐related subunits, with the opportunity to rapidly provide different analogues and structural variants for subsequent structure–function and associated biophysical investigations. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 60: 279–289, 2001</description><subject>Activins - chemistry</subject><subject>alpha-Macroglobulins - chemistry</subject><subject>Amino Acid Sequence</subject><subject>chemical synthesis</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Dose-Response Relationship, Drug</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>ESI-MS</subject><subject>Fluorenes - chemistry</subject><subject>Fmoc-solid</subject><subject>human activin βA[12-116]</subject><subject>Humans</subject><subject>Inhibin-beta Subunits - chemical synthesis</subject><subject>Inhibin-beta Subunits - chemistry</subject><subject>Kinetics</subject><subject>large-loop polypeptides</subject><subject>Molecular Sequence Data</subject><subject>Peptide Biosynthesis</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>phase methods</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Time Factors</subject><subject>Transformation, Genetic</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkduO0zAURS0EYsrALyA_IXhwOb4kjgtC6hQYKrUUxCBACB05iTs141yIU6C_xYfwTaRqZ3g6t332w16EaA5jDiCecjCagcjEYwHAn6QwUc-FNpPJdP6Snc3fGWPghRzDeLZ6JtjyFhndfNwmIwBImUxEckLuxfgdQCnJ4S454VxrJSQfkS8XTW8DLTau8sXQxF3db1z0kTZrutlWtqa26P1PX9O_f6ZfuWCcp9-orUvauWB7V9Jgu0vHQtO0tG3CrnVt70sX75M7axuie3Csp-Tj61cXszdssTqfz6YLdilVCizNc2kgk8JaJ7Ocq7Us8nVmrSxzm-nEcNBOJcOk0yJXVhYCuC4TY4V1ThXylDw6-LZd82PrYo-Vj4ULwdau2UbUQmaCy2QQPjwKt3nlSmw7X9luh9dhDIIPB8EvH9zu_x1wzwL3yeI-WdyzwBRQ4cACBxR4RIESAWcrFLi8Xg2u7ODqY-9-37ja7gpTLXWCn96e43utlgv-2eBC_gN3z4-o</recordid><startdate>2001</startdate><enddate>2001</enddate><creator>Keah, Hooi Hong</creator><creator>Allen, Natalie</creator><creator>Clay, Robert</creator><creator>Boysen, Reinhard I.</creator><creator>Warner, Tracy</creator><creator>Hearn, Milton T. W.</creator><general>John Wiley & Sons, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>2001</creationdate><title>Total chemical synthesis of human activin βA[12-116] and related large-loop polypeptides</title><author>Keah, Hooi Hong ; Allen, Natalie ; Clay, Robert ; Boysen, Reinhard I. ; Warner, Tracy ; Hearn, Milton T. W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g3460-6bb390832aae38b14f3cbf8aa3dba8759107e453db76cb4a3c2017d59a2aee4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Activins - chemistry</topic><topic>alpha-Macroglobulins - chemistry</topic><topic>Amino Acid Sequence</topic><topic>chemical synthesis</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Dose-Response Relationship, Drug</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>ESI-MS</topic><topic>Fluorenes - chemistry</topic><topic>Fmoc-solid</topic><topic>human activin βA[12-116]</topic><topic>Humans</topic><topic>Inhibin-beta Subunits - chemical synthesis</topic><topic>Inhibin-beta Subunits - chemistry</topic><topic>Kinetics</topic><topic>large-loop polypeptides</topic><topic>Molecular Sequence Data</topic><topic>Peptide Biosynthesis</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>phase methods</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Time Factors</topic><topic>Transformation, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Keah, Hooi Hong</creatorcontrib><creatorcontrib>Allen, Natalie</creatorcontrib><creatorcontrib>Clay, Robert</creatorcontrib><creatorcontrib>Boysen, Reinhard I.</creatorcontrib><creatorcontrib>Warner, Tracy</creatorcontrib><creatorcontrib>Hearn, Milton T. 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W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Total chemical synthesis of human activin βA[12-116] and related large-loop polypeptides</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>2001</date><risdate>2001</risdate><volume>60</volume><issue>4</issue><spage>279</spage><epage>289</epage><pages>279-289</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>We report here the synthesis, purification, and characterization of several large polypeptides related to the human activin βA subunit and their cyclic counterparts. In particular, we describe for the first time the total chemical synthesis of a 105‐mer polypeptide, des[1–11] activin βA, and related large‐loop polypeptide, by an optimized solid phase synthetic protocol based on 9‐flouroenylmethyoxycarbonyl (Fmoc) chemistry. These studies show that automated chemical synthesis utilizing Fmoc‐based solid phase synthetic strategies provides a practical alternative to recombinant DNA technology for the production of activin‐related subunits, with the opportunity to rapidly provide different analogues and structural variants for subsequent structure–function and associated biophysical investigations. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 60: 279–289, 2001</abstract><cop>New York</cop><pub>John Wiley & Sons, Inc</pub><pmid>11774231</pmid><doi>10.1002/1097-0282(2001)60:4<279::AID-BIP9990>3.0.CO;2-M</doi><tpages>11</tpages></addata></record> |
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subjects | Activins - chemistry alpha-Macroglobulins - chemistry Amino Acid Sequence chemical synthesis Chromatography, High Pressure Liquid Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel ESI-MS Fluorenes - chemistry Fmoc-solid human activin βA[12-116] Humans Inhibin-beta Subunits - chemical synthesis Inhibin-beta Subunits - chemistry Kinetics large-loop polypeptides Molecular Sequence Data Peptide Biosynthesis Peptides - chemical synthesis Peptides - chemistry phase methods Protein Binding Protein Conformation Time Factors Transformation, Genetic |
title | Total chemical synthesis of human activin βA[12-116] and related large-loop polypeptides |
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