TREN (Tris(2-aminoethyl)amine): An Effective Scaffold for the Assembly of Triple Helical Collagen Mimetic Structures
A new scaffold, TREN-(suc-OH)3 where TREN is tris(2-aminoethyl)amine and suc is the succinic acid spacers, was incorporated to assemble triple helices composed of Gly-Nleu-Pro sequences (Nleu denotes N-isobutylglycine). Extensive biophysical studies which include denaturation studies, CD and NMR spe...
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| Veröffentlicht in: | Journal of the American Chemical Society 2002-11, Vol.124 (47), p.14085-14091 |
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| container_end_page | 14091 |
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| container_issue | 47 |
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| container_title | Journal of the American Chemical Society |
| container_volume | 124 |
| creator | Kwak, Juliann Capua, Antonia De Locardi, Elsa Goodman, Murray |
| description | A new scaffold, TREN-(suc-OH)3 where TREN is tris(2-aminoethyl)amine and suc is the succinic acid spacers, was incorporated to assemble triple helices composed of Gly-Nleu-Pro sequences (Nleu denotes N-isobutylglycine). Extensive biophysical studies which include denaturation studies, CD and NMR spectroscopy, and molecular modeling demonstrated that TREN-[suc-(Gly-Nleu-Pro) n -NH2]3 (n = 5 and 6) form stable triple helical structures in solution. A comparative analysis of TREN-assembled and KTA-assembled collagen mimetics (KTA denotes Kemp triacid, 1,3,5-trimethylcyclohexane-1,3,5-tricarboxylic acid) indicates that the flexibility of the TREN scaffold is superior to the KTA scaffold in inducing triple helicity. This effect most likely arises from the flexibility of the TREN scaffold which allows the three peptide chains to adjust their register for a tighter triple helical packing. |
| doi_str_mv | 10.1021/ja0209621 |
| format | Article |
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Extensive biophysical studies which include denaturation studies, CD and NMR spectroscopy, and molecular modeling demonstrated that TREN-[suc-(Gly-Nleu-Pro) n -NH2]3 (n = 5 and 6) form stable triple helical structures in solution. A comparative analysis of TREN-assembled and KTA-assembled collagen mimetics (KTA denotes Kemp triacid, 1,3,5-trimethylcyclohexane-1,3,5-tricarboxylic acid) indicates that the flexibility of the TREN scaffold is superior to the KTA scaffold in inducing triple helicity. 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Am. Chem. Soc</addtitle><description>A new scaffold, TREN-(suc-OH)3 where TREN is tris(2-aminoethyl)amine and suc is the succinic acid spacers, was incorporated to assemble triple helices composed of Gly-Nleu-Pro sequences (Nleu denotes N-isobutylglycine). Extensive biophysical studies which include denaturation studies, CD and NMR spectroscopy, and molecular modeling demonstrated that TREN-[suc-(Gly-Nleu-Pro) n -NH2]3 (n = 5 and 6) form stable triple helical structures in solution. A comparative analysis of TREN-assembled and KTA-assembled collagen mimetics (KTA denotes Kemp triacid, 1,3,5-trimethylcyclohexane-1,3,5-tricarboxylic acid) indicates that the flexibility of the TREN scaffold is superior to the KTA scaffold in inducing triple helicity. This effect most likely arises from the flexibility of the TREN scaffold which allows the three peptide chains to adjust their register for a tighter triple helical packing.</description><subject>Analytical chemistry</subject><subject>Chemistry</subject><subject>Circular Dichroism</subject><subject>Collagen - chemistry</subject><subject>Ethylenediamines - chemistry</subject><subject>Exact sciences and technology</subject><subject>Models, Molecular</subject><subject>Molecular Mimicry</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - chemistry</subject><subject>Protein Denaturation</subject><subject>Protein Structure, Secondary</subject><subject>Spectrometric and optical methods</subject><subject>Thermodynamics</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM1uEzEURi0EoqGw4AWQN6BmMeDfmTG7KIS2qBREAiwtx7mmTmfGwZ6BZse2r8mT4CpRs2F1v6t79OnqIPSckteUMPpmbQgjqmT0ARpRyUghKSsfohEhhBVVXfIj9CSldV4Fq-ljdESZEESRaoR-L77MLvHJIvp0wgrT-i5Af7VtxncRxm___rnFkw7PnAPb-1-A59Y4F5oVdiHi_grwJCVol80WB4dzzaYBfAaNt6bB09A05gd0-KNvofcWz_s42H6IkJ6iR840CZ7t5zH6-n62mJ4VF59Oz6eTi8IIIftClJWsa-IsIStQKqc8KFcGqHKCE1sKWEkOnMgK6JJZYZyw1tVKCVsZy4_Rq13vJoafA6Retz5ZyH91EIakK1YqpSqewfEOtDGkFMHpTfStiVtNib6zrO8tZ_bFvnRYtrA6kHutGXi5B0zKIlw0nfXpwAleS8nqzBU7zqcebu7vJl7rsuKV1IvPc_2Nf5eX9MM7XR96jU16HYbYZXf_efAfpaufFg</recordid><startdate>20021127</startdate><enddate>20021127</enddate><creator>Kwak, Juliann</creator><creator>Capua, Antonia De</creator><creator>Locardi, Elsa</creator><creator>Goodman, Murray</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>20021127</creationdate><title>TREN (Tris(2-aminoethyl)amine): An Effective Scaffold for the Assembly of Triple Helical Collagen Mimetic Structures</title><author>Kwak, Juliann ; Capua, Antonia De ; Locardi, Elsa ; Goodman, Murray</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-4675880fc00de9980fde9139ae19f430c64ed53e3057e1b2c4af4ccf8994c7ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Analytical chemistry</topic><topic>Chemistry</topic><topic>Circular Dichroism</topic><topic>Collagen - chemistry</topic><topic>Ethylenediamines - chemistry</topic><topic>Exact sciences and technology</topic><topic>Models, Molecular</topic><topic>Molecular Mimicry</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - chemistry</topic><topic>Protein Denaturation</topic><topic>Protein Structure, Secondary</topic><topic>Spectrometric and optical methods</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kwak, Juliann</creatorcontrib><creatorcontrib>Capua, Antonia De</creatorcontrib><creatorcontrib>Locardi, Elsa</creatorcontrib><creatorcontrib>Goodman, Murray</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</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>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kwak, Juliann</au><au>Capua, Antonia De</au><au>Locardi, Elsa</au><au>Goodman, Murray</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TREN (Tris(2-aminoethyl)amine): An Effective Scaffold for the Assembly of Triple Helical Collagen Mimetic Structures</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2002-11-27</date><risdate>2002</risdate><volume>124</volume><issue>47</issue><spage>14085</spage><epage>14091</epage><pages>14085-14091</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>A new scaffold, TREN-(suc-OH)3 where TREN is tris(2-aminoethyl)amine and suc is the succinic acid spacers, was incorporated to assemble triple helices composed of Gly-Nleu-Pro sequences (Nleu denotes N-isobutylglycine). Extensive biophysical studies which include denaturation studies, CD and NMR spectroscopy, and molecular modeling demonstrated that TREN-[suc-(Gly-Nleu-Pro) n -NH2]3 (n = 5 and 6) form stable triple helical structures in solution. A comparative analysis of TREN-assembled and KTA-assembled collagen mimetics (KTA denotes Kemp triacid, 1,3,5-trimethylcyclohexane-1,3,5-tricarboxylic acid) indicates that the flexibility of the TREN scaffold is superior to the KTA scaffold in inducing triple helicity. This effect most likely arises from the flexibility of the TREN scaffold which allows the three peptide chains to adjust their register for a tighter triple helical packing.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12440907</pmid><doi>10.1021/ja0209621</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Analytical chemistry Chemistry Circular Dichroism Collagen - chemistry Ethylenediamines - chemistry Exact sciences and technology Models, Molecular Molecular Mimicry Nuclear Magnetic Resonance, Biomolecular Oligopeptides - chemical synthesis Oligopeptides - chemistry Protein Denaturation Protein Structure, Secondary Spectrometric and optical methods Thermodynamics |
| title | TREN (Tris(2-aminoethyl)amine): An Effective Scaffold for the Assembly of Triple Helical Collagen Mimetic Structures |
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