Marked Difference Between Self-aggregations of First and Fourth Repeat Peptides on Tau Microtubule-binding Domain in Acidic Solution
The heparin-induced self-aggregation behaviours of four repeat peptides (R1-R4) in an acidic solution (pH = 4.5) were investigated by fluorescence and circular dichroism (CD) measurements and compared with those in a neutral solution (pH = 7.5). In contrast with the self-aggregation-resistive behavi...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2007-07, Vol.142 (1), p.49-54 |
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| container_title | Journal of biochemistry (Tokyo) |
| container_volume | 142 |
| creator | Mizushima, Fumie Minoura, Katsuhiko Tomoo, Koji Sumida, Miho Taniguchi, Taizo Ishida, Toshimasa |
| description | The heparin-induced self-aggregation behaviours of four repeat peptides (R1-R4) in an acidic solution (pH = 4.5) were investigated by fluorescence and circular dichroism (CD) measurements and compared with those in a neutral solution (pH = 7.5). In contrast with the self-aggregation-resistive behaviours of the R1 and R4 repeat peptides in the neutral solution, the R4 peptide formed a filament similarly to the R2 and R3 peptides in the acidic solution, whereas the R1 peptide still showed resistive behaviour for filament formation. This is the first report on the markedly different self-aggregation behaviours of the first and fourth repeat peptides on tau microtubule-binding domain. |
| doi_str_mv | 10.1093/jb/mvm099 |
| format | Article |
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In contrast with the self-aggregation-resistive behaviours of the R1 and R4 repeat peptides in the neutral solution, the R4 peptide formed a filament similarly to the R2 and R3 peptides in the acidic solution, whereas the R1 peptide still showed resistive behaviour for filament formation. This is the first report on the markedly different self-aggregation behaviours of the first and fourth repeat peptides on tau microtubule-binding domain.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvm099</identifier><identifier>PMID: 17456500</identifier><language>eng</language><publisher>England: Japanese Biochemical Society</publisher><subject>Amino Acid Sequence ; Binding Sites ; Circular Dichroism ; conformational transition ; filament formation ; Heparin - metabolism ; Hydrogen-Ion Concentration ; Microscopy, Electron ; microtubule-binding domain ; Microtubules - chemistry ; Microtubules - metabolism ; Molecular Sequence Data ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - metabolism ; Protein Conformation ; Protein Structure, Tertiary ; repeat peptide ; Repetitive Sequences, Amino Acid ; Solutions - metabolism ; Spectrometry, Fluorescence ; tau ; tau Proteins - chemistry ; tau Proteins - metabolism ; Time Factors</subject><ispartof>Journal of biochemistry (Tokyo), 2007-07, Vol.142 (1), p.49-54</ispartof><rights>2007 The Japanese Biochemical Society. 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c489t-7d8cf56f4cc2ae3ddecf320b48fa999612a31baf13f63ffb7dd91b64366416a23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17456500$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mizushima, Fumie</creatorcontrib><creatorcontrib>Minoura, Katsuhiko</creatorcontrib><creatorcontrib>Tomoo, Koji</creatorcontrib><creatorcontrib>Sumida, Miho</creatorcontrib><creatorcontrib>Taniguchi, Taizo</creatorcontrib><creatorcontrib>Ishida, Toshimasa</creatorcontrib><title>Marked Difference Between Self-aggregations of First and Fourth Repeat Peptides on Tau Microtubule-binding Domain in Acidic Solution</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The heparin-induced self-aggregation behaviours of four repeat peptides (R1-R4) in an acidic solution (pH = 4.5) were investigated by fluorescence and circular dichroism (CD) measurements and compared with those in a neutral solution (pH = 7.5). In contrast with the self-aggregation-resistive behaviours of the R1 and R4 repeat peptides in the neutral solution, the R4 peptide formed a filament similarly to the R2 and R3 peptides in the acidic solution, whereas the R1 peptide still showed resistive behaviour for filament formation. This is the first report on the markedly different self-aggregation behaviours of the first and fourth repeat peptides on tau microtubule-binding domain.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Circular Dichroism</subject><subject>conformational transition</subject><subject>filament formation</subject><subject>Heparin - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Microscopy, Electron</subject><subject>microtubule-binding domain</subject><subject>Microtubules - chemistry</subject><subject>Microtubules - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>repeat peptide</subject><subject>Repetitive Sequences, Amino Acid</subject><subject>Solutions - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>tau</subject><subject>tau Proteins - chemistry</subject><subject>tau Proteins - metabolism</subject><subject>Time Factors</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90cuKFDEUBuAgitOOLnwBzUIEF-XkVqmq5VxsW5hBsWewcRNSyUmZtm4mKS97H9xqqtGdEDgEPn44_0HoKSWvKan42b4-6753pKruoRUtcpkxmdP7aEUIo1nFxO4EPYpxf_gyzh-iE1qIXOaErNDvGx2-gsVX3jkI0BvAF5B-APR4C63LdNMEaHTyQx_x4PDah5iw7i1eD1NIX_BHGEEn_AHG5C3Mpse3esI33oQhTfXUQlb73vq-wVdDp32P53duvPUGb4d2OiQ_Rg-cbiM8Oc5TdLd-c3u5ya7fv313eX6dGVFWKStsaVwunTCGaeDWgnGckVqUTldVJSnTnNbaUe4kd64urK1oLQWXUlCpGT9FL5fcMQzfJohJdT4aaFvdwzBFJUsqaJ4f4KsFzkvEGMCpMfhOh1-KEnWoXO1rtVQ-22fH0KnuwP6Tx45n8GIBwzT-NydbmI8Jfv6F83mULHiRq83us9rIUuxkuVafZv988U4PSjfBR3W3ZYRyQoqqIILxP2bSo3k</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Mizushima, Fumie</creator><creator>Minoura, Katsuhiko</creator><creator>Tomoo, Koji</creator><creator>Sumida, Miho</creator><creator>Taniguchi, Taizo</creator><creator>Ishida, Toshimasa</creator><general>Japanese Biochemical Society</general><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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>20070701</creationdate><title>Marked Difference Between Self-aggregations of First and Fourth Repeat Peptides on Tau Microtubule-binding Domain in Acidic Solution</title><author>Mizushima, Fumie ; Minoura, Katsuhiko ; Tomoo, Koji ; Sumida, Miho ; Taniguchi, Taizo ; Ishida, Toshimasa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c489t-7d8cf56f4cc2ae3ddecf320b48fa999612a31baf13f63ffb7dd91b64366416a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Circular Dichroism</topic><topic>conformational transition</topic><topic>filament formation</topic><topic>Heparin - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Microscopy, Electron</topic><topic>microtubule-binding domain</topic><topic>Microtubules - chemistry</topic><topic>Microtubules - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>repeat peptide</topic><topic>Repetitive Sequences, Amino Acid</topic><topic>Solutions - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>tau</topic><topic>tau Proteins - chemistry</topic><topic>tau Proteins - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mizushima, Fumie</creatorcontrib><creatorcontrib>Minoura, Katsuhiko</creatorcontrib><creatorcontrib>Tomoo, Koji</creatorcontrib><creatorcontrib>Sumida, Miho</creatorcontrib><creatorcontrib>Taniguchi, Taizo</creatorcontrib><creatorcontrib>Ishida, Toshimasa</creatorcontrib><collection>AGRIS</collection><collection>Istex</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 biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mizushima, Fumie</au><au>Minoura, Katsuhiko</au><au>Tomoo, Koji</au><au>Sumida, Miho</au><au>Taniguchi, Taizo</au><au>Ishida, Toshimasa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Marked Difference Between Self-aggregations of First and Fourth Repeat Peptides on Tau Microtubule-binding Domain in Acidic Solution</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>142</volume><issue>1</issue><spage>49</spage><epage>54</epage><pages>49-54</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>The heparin-induced self-aggregation behaviours of four repeat peptides (R1-R4) in an acidic solution (pH = 4.5) were investigated by fluorescence and circular dichroism (CD) measurements and compared with those in a neutral solution (pH = 7.5). In contrast with the self-aggregation-resistive behaviours of the R1 and R4 repeat peptides in the neutral solution, the R4 peptide formed a filament similarly to the R2 and R3 peptides in the acidic solution, whereas the R1 peptide still showed resistive behaviour for filament formation. This is the first report on the markedly different self-aggregation behaviours of the first and fourth repeat peptides on tau microtubule-binding domain.</abstract><cop>England</cop><pub>Japanese Biochemical Society</pub><pmid>17456500</pmid><doi>10.1093/jb/mvm099</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of biochemistry (Tokyo), 2007-07, Vol.142 (1), p.49-54 |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE |
| subjects | Amino Acid Sequence Binding Sites Circular Dichroism conformational transition filament formation Heparin - metabolism Hydrogen-Ion Concentration Microscopy, Electron microtubule-binding domain Microtubules - chemistry Microtubules - metabolism Molecular Sequence Data Peptides - chemical synthesis Peptides - chemistry Peptides - metabolism Protein Conformation Protein Structure, Tertiary repeat peptide Repetitive Sequences, Amino Acid Solutions - metabolism Spectrometry, Fluorescence tau tau Proteins - chemistry tau Proteins - metabolism Time Factors |
| title | Marked Difference Between Self-aggregations of First and Fourth Repeat Peptides on Tau Microtubule-binding Domain in Acidic Solution |
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