The folding of a metallopeptide
We have applied solid-phase synthesis methods for the construction of tris(bipyridyl) peptidic ligands that coordinate Fe( ii ) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around...
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| Veröffentlicht in: | Dalton transactions : an international journal of inorganic chemistry 2016-01, Vol.45 (3), p.881-885 |
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| container_title | Dalton transactions : an international journal of inorganic chemistry |
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| creator | Gamba, Ilaria Rama, Gustavo Ortega-Carrasco, Elisabeth Berardozzi, Roberto Sánchez-Pedregal, Víctor M Di Bari, Lorenzo Maréchal, Jean-Didier Vázquez, M. Eugenio Vázquez López, Miguel |
| description | We have applied solid-phase synthesis methods for the construction of tris(bipyridyl) peptidic ligands that coordinate Fe(
ii
) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around the metal ions have been studied both by experimental techniques (CD, UV-vis and NMR) and molecular modeling tools. Amongst the numerous molecular variables that have been studied, this study clearly illustrates how the chirality of a given set of aminoacids (proline in this case) of the peptide dictates the chirality of the metal center of the resulting metallopeptide. Moreover, the relatively hydrophobic peptidic models used in this work show that the most stable structures present reduced solvent contacts and, in counterpart, stabilize the
cis
configuration of the proline residues.
We have studied the main factors influencing the folding pathway and chiral control of a family of tris(bipyridyl) peptidic ligands in the presence of Fe(
ii
) ions both by experimental techniques and molecular modeling tools. |
| doi_str_mv | 10.1039/c5dt02797g |
| format | Article |
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ii
) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around the metal ions have been studied both by experimental techniques (CD, UV-vis and NMR) and molecular modeling tools. Amongst the numerous molecular variables that have been studied, this study clearly illustrates how the chirality of a given set of aminoacids (proline in this case) of the peptide dictates the chirality of the metal center of the resulting metallopeptide. Moreover, the relatively hydrophobic peptidic models used in this work show that the most stable structures present reduced solvent contacts and, in counterpart, stabilize the
cis
configuration of the proline residues.
We have studied the main factors influencing the folding pathway and chiral control of a family of tris(bipyridyl) peptidic ligands in the presence of Fe(
ii
) ions both by experimental techniques and molecular modeling tools.</description><identifier>ISSN: 1477-9226</identifier><identifier>EISSN: 1477-9234</identifier><identifier>DOI: 10.1039/c5dt02797g</identifier><identifier>PMID: 26523378</identifier><language>eng</language><publisher>England</publisher><subject>2,2'-Dipyridyl - chemistry ; Chirality ; Contact ; Ferrous Compounds - chemistry ; Folding ; Ligands ; Mathematical models ; Metalloproteins - chemistry ; Molecular Structure ; Peptides - chemistry ; Proline ; Protein Folding ; Quantum Theory ; Residues ; Solvents</subject><ispartof>Dalton transactions : an international journal of inorganic chemistry, 2016-01, Vol.45 (3), p.881-885</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-7377ee1e1db825092e16a6003d49cc6e84447c641e5737724d81a9f9725ee7223</citedby><cites>FETCH-LOGICAL-c378t-7377ee1e1db825092e16a6003d49cc6e84447c641e5737724d81a9f9725ee7223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26523378$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gamba, Ilaria</creatorcontrib><creatorcontrib>Rama, Gustavo</creatorcontrib><creatorcontrib>Ortega-Carrasco, Elisabeth</creatorcontrib><creatorcontrib>Berardozzi, Roberto</creatorcontrib><creatorcontrib>Sánchez-Pedregal, Víctor M</creatorcontrib><creatorcontrib>Di Bari, Lorenzo</creatorcontrib><creatorcontrib>Maréchal, Jean-Didier</creatorcontrib><creatorcontrib>Vázquez, M. Eugenio</creatorcontrib><creatorcontrib>Vázquez López, Miguel</creatorcontrib><title>The folding of a metallopeptide</title><title>Dalton transactions : an international journal of inorganic chemistry</title><addtitle>Dalton Trans</addtitle><description>We have applied solid-phase synthesis methods for the construction of tris(bipyridyl) peptidic ligands that coordinate Fe(
ii
) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around the metal ions have been studied both by experimental techniques (CD, UV-vis and NMR) and molecular modeling tools. Amongst the numerous molecular variables that have been studied, this study clearly illustrates how the chirality of a given set of aminoacids (proline in this case) of the peptide dictates the chirality of the metal center of the resulting metallopeptide. Moreover, the relatively hydrophobic peptidic models used in this work show that the most stable structures present reduced solvent contacts and, in counterpart, stabilize the
cis
configuration of the proline residues.
We have studied the main factors influencing the folding pathway and chiral control of a family of tris(bipyridyl) peptidic ligands in the presence of Fe(
ii
) ions both by experimental techniques and molecular modeling tools.</description><subject>2,2'-Dipyridyl - chemistry</subject><subject>Chirality</subject><subject>Contact</subject><subject>Ferrous Compounds - chemistry</subject><subject>Folding</subject><subject>Ligands</subject><subject>Mathematical models</subject><subject>Metalloproteins - chemistry</subject><subject>Molecular Structure</subject><subject>Peptides - chemistry</subject><subject>Proline</subject><subject>Protein Folding</subject><subject>Quantum Theory</subject><subject>Residues</subject><subject>Solvents</subject><issn>1477-9226</issn><issn>1477-9234</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0D9PwzAQhnELgWgpLOxARoQUOP_LxSMKUJAqsZQ5cu1LCUqaEKcD356UljIy-ST_9A4PY-ccbjlIc-e070GgweUBG3OFGBsh1eH-FsmInYTwASAEaHHMRiLRQkpMx-xq_k5R0VS-XC2jpohsVFNvq6ppqe1LT6fsqLBVoLPdO2FvT4_z7DmevU5fsvtZ7IaZPkaJSMSJ-0UqNBhBPLEJgPTKOJdQqpRClyhOekOF8im3pjAoNBEKISfservbds3nmkKf12VwVFV2Rc065DyFFDRqxP8pagVGGoSB3myp65oQOirytitr233lHPJNuzzTD_OfdtMBX-5214ua_J7-xhrAxRZ0we1__-LLb0e5b7k</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Gamba, Ilaria</creator><creator>Rama, Gustavo</creator><creator>Ortega-Carrasco, Elisabeth</creator><creator>Berardozzi, Roberto</creator><creator>Sánchez-Pedregal, Víctor M</creator><creator>Di Bari, Lorenzo</creator><creator>Maréchal, Jean-Didier</creator><creator>Vázquez, M. Eugenio</creator><creator>Vázquez López, Miguel</creator><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><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20160101</creationdate><title>The folding of a metallopeptide</title><author>Gamba, Ilaria ; Rama, Gustavo ; Ortega-Carrasco, Elisabeth ; Berardozzi, Roberto ; Sánchez-Pedregal, Víctor M ; Di Bari, Lorenzo ; Maréchal, Jean-Didier ; Vázquez, M. Eugenio ; Vázquez López, Miguel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-7377ee1e1db825092e16a6003d49cc6e84447c641e5737724d81a9f9725ee7223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>2,2'-Dipyridyl - chemistry</topic><topic>Chirality</topic><topic>Contact</topic><topic>Ferrous Compounds - chemistry</topic><topic>Folding</topic><topic>Ligands</topic><topic>Mathematical models</topic><topic>Metalloproteins - chemistry</topic><topic>Molecular Structure</topic><topic>Peptides - chemistry</topic><topic>Proline</topic><topic>Protein Folding</topic><topic>Quantum Theory</topic><topic>Residues</topic><topic>Solvents</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gamba, Ilaria</creatorcontrib><creatorcontrib>Rama, Gustavo</creatorcontrib><creatorcontrib>Ortega-Carrasco, Elisabeth</creatorcontrib><creatorcontrib>Berardozzi, Roberto</creatorcontrib><creatorcontrib>Sánchez-Pedregal, Víctor M</creatorcontrib><creatorcontrib>Di Bari, Lorenzo</creatorcontrib><creatorcontrib>Maréchal, Jean-Didier</creatorcontrib><creatorcontrib>Vázquez, M. Eugenio</creatorcontrib><creatorcontrib>Vázquez López, Miguel</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><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Dalton transactions : an international journal of inorganic chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gamba, Ilaria</au><au>Rama, Gustavo</au><au>Ortega-Carrasco, Elisabeth</au><au>Berardozzi, Roberto</au><au>Sánchez-Pedregal, Víctor M</au><au>Di Bari, Lorenzo</au><au>Maréchal, Jean-Didier</au><au>Vázquez, M. Eugenio</au><au>Vázquez López, Miguel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The folding of a metallopeptide</atitle><jtitle>Dalton transactions : an international journal of inorganic chemistry</jtitle><addtitle>Dalton Trans</addtitle><date>2016-01-01</date><risdate>2016</risdate><volume>45</volume><issue>3</issue><spage>881</spage><epage>885</epage><pages>881-885</pages><issn>1477-9226</issn><eissn>1477-9234</eissn><abstract>We have applied solid-phase synthesis methods for the construction of tris(bipyridyl) peptidic ligands that coordinate Fe(
ii
) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around the metal ions have been studied both by experimental techniques (CD, UV-vis and NMR) and molecular modeling tools. Amongst the numerous molecular variables that have been studied, this study clearly illustrates how the chirality of a given set of aminoacids (proline in this case) of the peptide dictates the chirality of the metal center of the resulting metallopeptide. Moreover, the relatively hydrophobic peptidic models used in this work show that the most stable structures present reduced solvent contacts and, in counterpart, stabilize the
cis
configuration of the proline residues.
We have studied the main factors influencing the folding pathway and chiral control of a family of tris(bipyridyl) peptidic ligands in the presence of Fe(
ii
) ions both by experimental techniques and molecular modeling tools.</abstract><cop>England</cop><pmid>26523378</pmid><doi>10.1039/c5dt02797g</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1477-9226 |
| ispartof | Dalton transactions : an international journal of inorganic chemistry, 2016-01, Vol.45 (3), p.881-885 |
| issn | 1477-9226 1477-9234 |
| language | eng |
| recordid | cdi_rsc_primary_c5dt02797g |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | 2,2'-Dipyridyl - chemistry Chirality Contact Ferrous Compounds - chemistry Folding Ligands Mathematical models Metalloproteins - chemistry Molecular Structure Peptides - chemistry Proline Protein Folding Quantum Theory Residues Solvents |
| title | The folding of a metallopeptide |
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