Multiple glycosylation of de novo designed α-helical coiled coil peptides
The aim of this study was to investigate the influence of multiple O-glycosylation in α-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six β-galactose residues into the solvent exposed positions of a 26 amino acid long coiled coil he...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2010-06, Vol.18 (11), p.3703-3706 |
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| container_title | Bioorganic & medicinal chemistry |
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| creator | Falenski, Jessica A. Gerling, Ulla I.M. Koksch, Beate |
| description | The aim of this study was to investigate the influence of multiple O-glycosylation in α-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six β-galactose residues into the solvent exposed positions of a 26 amino acid long coiled coil helix. Surprisingly, circular dichroism spectroscopy showed no unfolding of the coiled coil structure for all glycopeptides. Thermally induced denaturations reveal a successive but relative low destabilization of the coiled coil structure upon introduction of β-galactose residues. These first results indicate that
O-glycosylation of the glycosylated variants is easily tolerated by this structural motif and pave the way for further functional studies. |
| doi_str_mv | 10.1016/j.bmc.2010.03.061 |
| format | Article |
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O-glycosylation of the glycosylated variants is easily tolerated by this structural motif and pave the way for further functional studies.</description><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chemistry</subject><subject>Circular Dichroism</subject><subject>Drug Design</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactose - chemistry</subject><subject>Glycopeptide</subject><subject>Glycopeptides - chemical synthesis</subject><subject>Glycopeptides - chemistry</subject><subject>Glycosylation</subject><subject>Helix</subject><subject>Organic chemistry</subject><subject>Peptides</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Post-translational modification</subject><subject>Preparations and properties</subject><subject>Protein Denaturation</subject><subject>Protein Stability</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Solid phase synthesis</subject><issn>0968-0896</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFOGzEQhq0K1KTAA_SC9oI4bRjPbLy2eqoQlCIQl_ZsOV5v6shZb9cbpDwWL8Iz4SiB3nr6NaNvRjMfY185zDhwcbWaLdZ2hpBroBkI_olNeSWqkkjxIzYFJWQJUokJ-5LSCgCwUvwzmyDMOQmqp-z-cRNG3wdXLMPWxrQNZvSxK2JbNK7o4nPMmfyyc03x-lL-ccFbEwobfcidXRS960efoVN23JqQ3NkhT9jv25tf13flw9OPn9ffH0pLEseSsEKspSSqpJzbqm6hBYu1opqjmVuQVoo5CWxaBLEwilQDNTb5jUVrjKATdrnf2w_x78alUa99si4E07m4Sbom4lgDqEzyPWmHmNLgWt0Pfm2Greagdwb1SmeDemdQA-lsMM-cH7ZvFmvXfEy8K8vAxQEwKatoB9NZn_5xqACRMHPf9pzLLp69G3Sy3nXWNX5wdtRN9P854w1jn4zv</recordid><startdate>20100601</startdate><enddate>20100601</enddate><creator>Falenski, Jessica A.</creator><creator>Gerling, Ulla I.M.</creator><creator>Koksch, Beate</creator><general>Elsevier Ltd</general><general>Elsevier</general><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>20100601</creationdate><title>Multiple glycosylation of de novo designed α-helical coiled coil peptides</title><author>Falenski, Jessica A. ; Gerling, Ulla I.M. ; Koksch, Beate</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-32422788334885c47f0f0c2793712a5c08c865362df206ba939d072d896bfaa63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chemistry</topic><topic>Circular Dichroism</topic><topic>Drug Design</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactose - chemistry</topic><topic>Glycopeptide</topic><topic>Glycopeptides - chemical synthesis</topic><topic>Glycopeptides - chemistry</topic><topic>Glycosylation</topic><topic>Helix</topic><topic>Organic chemistry</topic><topic>Peptides</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Post-translational modification</topic><topic>Preparations and properties</topic><topic>Protein Denaturation</topic><topic>Protein Stability</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Solid phase synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Falenski, Jessica A.</creatorcontrib><creatorcontrib>Gerling, Ulla I.M.</creatorcontrib><creatorcontrib>Koksch, Beate</creatorcontrib><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>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Falenski, Jessica A.</au><au>Gerling, Ulla I.M.</au><au>Koksch, Beate</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple glycosylation of de novo designed α-helical coiled coil peptides</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>2010-06-01</date><risdate>2010</risdate><volume>18</volume><issue>11</issue><spage>3703</spage><epage>3706</epage><pages>3703-3706</pages><issn>0968-0896</issn><eissn>1464-3391</eissn><abstract>The aim of this study was to investigate the influence of multiple O-glycosylation in α-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six β-galactose residues into the solvent exposed positions of a 26 amino acid long coiled coil helix. Surprisingly, circular dichroism spectroscopy showed no unfolding of the coiled coil structure for all glycopeptides. Thermally induced denaturations reveal a successive but relative low destabilization of the coiled coil structure upon introduction of β-galactose residues. These first results indicate that
O-glycosylation of the glycosylated variants is easily tolerated by this structural motif and pave the way for further functional studies.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>20513637</pmid><doi>10.1016/j.bmc.2010.03.061</doi><tpages>4</tpages></addata></record> |
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| language | eng |
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| subjects | Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences Chemistry Circular Dichroism Drug Design Exact sciences and technology Fundamental and applied biological sciences. Psychology Galactose - chemistry Glycopeptide Glycopeptides - chemical synthesis Glycopeptides - chemistry Glycosylation Helix Organic chemistry Peptides Peptides - chemical synthesis Peptides - chemistry Post-translational modification Preparations and properties Protein Denaturation Protein Stability Protein Structure, Secondary Proteins Solid phase synthesis |
| title | Multiple glycosylation of de novo designed α-helical coiled coil peptides |
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