Effect of polyanions on the unfolding of acidic fibroblast growth factor
The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. In the absence of a stabilizing polyanion, the apparent free energy of unfolding of aFGF is 6.5 kcal mol-1. The presen...
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| Veröffentlicht in: | Biochemistry (Easton) 1993-06, Vol.32 (25), p.6419-6426 |
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| creator | Burke, Carl J Volkin, David B Mach, Henryk Middaugh, C. Russell |
| description | The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. In the absence of a stabilizing polyanion, the apparent free energy of unfolding of aFGF is 6.5 kcal mol-1. The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold. The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. The presence of similar amounts of other polyanions such as sulfated beta-cyclodextrin or heparan sulfate also stabilizes aFGF to a similar extent as heparin. Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. |
| doi_str_mv | 10.1021/bi00076a015 |
| format | Article |
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Russell</creator><creatorcontrib>Burke, Carl J ; Volkin, David B ; Mach, Henryk ; Middaugh, C. Russell</creatorcontrib><description>The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. In the absence of a stabilizing polyanion, the apparent free energy of unfolding of aFGF is 6.5 kcal mol-1. The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold. The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. The presence of similar amounts of other polyanions such as sulfated beta-cyclodextrin or heparan sulfate also stabilizes aFGF to a similar extent as heparin. Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00076a015</identifier><identifier>PMID: 7686045</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; beta-Cyclodextrins ; Biological and medical sciences ; Calorimetry ; Circular Dichroism ; Cyclodextrins - pharmacology ; Fibroblast Growth Factor 1 - chemistry ; Fibroblast Growth Factor 1 - drug effects ; Fibroblast Growth Factor 1 - metabolism ; Fundamental and applied biological sciences. Psychology ; Heparin - pharmacology ; Heparitin Sulfate - pharmacology ; Humans ; Inositol - pharmacology ; Intermediary metabolites. Miscellaneous ; Other biological molecules ; Phytic Acid - pharmacology ; Protein Denaturation ; Protein Folding ; Recombinant Proteins - chemistry ; Recombinant Proteins - drug effects ; Recombinant Proteins - metabolism ; Spectrometry, Fluorescence ; Urea - pharmacology</subject><ispartof>Biochemistry (Easton), 1993-06, Vol.32 (25), p.6419-6426</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a383t-ca2d7c955776074e698fd420939554683c486f243a5920d06180bd8d9d753bd83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00076a015$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00076a015$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4853079$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7686045$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Burke, Carl J</creatorcontrib><creatorcontrib>Volkin, David B</creatorcontrib><creatorcontrib>Mach, Henryk</creatorcontrib><creatorcontrib>Middaugh, C. Russell</creatorcontrib><title>Effect of polyanions on the unfolding of acidic fibroblast growth factor</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. In the absence of a stabilizing polyanion, the apparent free energy of unfolding of aFGF is 6.5 kcal mol-1. The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold. The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. The presence of similar amounts of other polyanions such as sulfated beta-cyclodextrin or heparan sulfate also stabilizes aFGF to a similar extent as heparin. Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>beta-Cyclodextrins</subject><subject>Biological and medical sciences</subject><subject>Calorimetry</subject><subject>Circular Dichroism</subject><subject>Cyclodextrins - pharmacology</subject><subject>Fibroblast Growth Factor 1 - chemistry</subject><subject>Fibroblast Growth Factor 1 - drug effects</subject><subject>Fibroblast Growth Factor 1 - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heparin - pharmacology</subject><subject>Heparitin Sulfate - pharmacology</subject><subject>Humans</subject><subject>Inositol - pharmacology</subject><subject>Intermediary metabolites. Miscellaneous</subject><subject>Other biological molecules</subject><subject>Phytic Acid - pharmacology</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - drug effects</subject><subject>Recombinant Proteins - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Urea - pharmacology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkEtLAzEUhYMotT5WroUsBBcympm8l-IbahWs65BJJjZ1nJRkivrvjUwpLlzdx_m4nHsAOCrReYmq8qL2CCHONCrpFhiXtEIFkZJug3Hes6KSDO2CvZQWeSSIkxEYcSYYInQM7m-ca0wPg4PL0H7rzocuwdDBft7AVedCa3339itr46030Pk6hrrVqYdvMXz2c-i06UM8ADtOt6k5XNd98Hp7M7u6LyZPdw9Xl5NCY4H7wujKciMp5ZxlKw2TwllSIYnzjjCBDRHMVQRrKitkESsFqq2w0nKKc4P3wdlw18SQUmycWkb_oeO3KpH6jUP9iSPTxwO9XNUfjd2w6_-zfrLWdTK6dVF3xqcNRgTFiMuMFQPmU998bWQd3xXjmFM1e35R09lUPE7Ka3Wb-dOB1yapRVjFLkfyr8Ef6BuBRA</recordid><startdate>19930629</startdate><enddate>19930629</enddate><creator>Burke, Carl J</creator><creator>Volkin, David B</creator><creator>Mach, Henryk</creator><creator>Middaugh, C. Russell</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></search><sort><creationdate>19930629</creationdate><title>Effect of polyanions on the unfolding of acidic fibroblast growth factor</title><author>Burke, Carl J ; Volkin, David B ; Mach, Henryk ; Middaugh, C. Russell</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a383t-ca2d7c955776074e698fd420939554683c486f243a5920d06180bd8d9d753bd83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>beta-Cyclodextrins</topic><topic>Biological and medical sciences</topic><topic>Calorimetry</topic><topic>Circular Dichroism</topic><topic>Cyclodextrins - pharmacology</topic><topic>Fibroblast Growth Factor 1 - chemistry</topic><topic>Fibroblast Growth Factor 1 - drug effects</topic><topic>Fibroblast Growth Factor 1 - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heparin - pharmacology</topic><topic>Heparitin Sulfate - pharmacology</topic><topic>Humans</topic><topic>Inositol - pharmacology</topic><topic>Intermediary metabolites. Miscellaneous</topic><topic>Other biological molecules</topic><topic>Phytic Acid - pharmacology</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - drug effects</topic><topic>Recombinant Proteins - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Urea - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Burke, Carl J</creatorcontrib><creatorcontrib>Volkin, David B</creatorcontrib><creatorcontrib>Mach, Henryk</creatorcontrib><creatorcontrib>Middaugh, C. 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Russell</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of polyanions on the unfolding of acidic fibroblast growth factor</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1993-06-29</date><risdate>1993</risdate><volume>32</volume><issue>25</issue><spage>6419</spage><epage>6426</epage><pages>6419-6426</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. In the absence of a stabilizing polyanion, the apparent free energy of unfolding of aFGF is 6.5 kcal mol-1. The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold. The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. The presence of similar amounts of other polyanions such as sulfated beta-cyclodextrin or heparan sulfate also stabilizes aFGF to a similar extent as heparin. Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>7686045</pmid><doi>10.1021/bi00076a015</doi><tpages>8</tpages></addata></record> |
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| source | ACS Publications; MEDLINE |
| subjects | Analytical, structural and metabolic biochemistry beta-Cyclodextrins Biological and medical sciences Calorimetry Circular Dichroism Cyclodextrins - pharmacology Fibroblast Growth Factor 1 - chemistry Fibroblast Growth Factor 1 - drug effects Fibroblast Growth Factor 1 - metabolism Fundamental and applied biological sciences. Psychology Heparin - pharmacology Heparitin Sulfate - pharmacology Humans Inositol - pharmacology Intermediary metabolites. Miscellaneous Other biological molecules Phytic Acid - pharmacology Protein Denaturation Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - drug effects Recombinant Proteins - metabolism Spectrometry, Fluorescence Urea - pharmacology |
| title | Effect of polyanions on the unfolding of acidic fibroblast growth factor |
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