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Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6 and AcPHF6
In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs via the interaction of two hexapeptide motifs PHF* 275 VQIINK 280 and PHF 306 VQIVYK 311 as β-sheets. To understand the role of the constituent amino acids of PHF and PHF*...
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| Published in: | RSC advances 2020-07, Vol.1 (46), p.27331-27335 |
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| Main Authors: | , , , , , , |
| Format: | Article |
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| container_issue | 46 |
| container_start_page | 27331 |
| container_title | RSC advances |
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| creator | Dangi, Abha Balmik, Abhishek Ankur Ghorpade, Archana Kisan Gorantla, Nalini Vijay Sonawane, Shweta Kishor Chinnathambi, Subashchandrabose Marelli, Udaya Kiran |
| description | In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs
via
the interaction of two hexapeptide motifs PHF*
275
VQIINK
280
and PHF
306
VQIVYK
311
as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization.
In the alanine mutant peptides of AcPHF6* and AcPHF6, only the peptides with glutamine to alanine substitution show aggregation akin to that of the parent peptides. |
| doi_str_mv | 10.1039/d0ra03809a |
| format | article |
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via
the interaction of two hexapeptide motifs PHF*
275
VQIINK
280
and PHF
306
VQIVYK
311
as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization.
In the alanine mutant peptides of AcPHF6* and AcPHF6, only the peptides with glutamine to alanine substitution show aggregation akin to that of the parent peptides.</description><identifier>ISSN: 2046-2069</identifier><identifier>EISSN: 2046-2069</identifier><identifier>DOI: 10.1039/d0ra03809a</identifier><identifier>PMID: 35516938</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Agglomeration ; Alanine ; Alzheimer's disease ; Amino acids ; Chemistry ; Dichroism ; Fluorescence ; Glutamine ; Morphology ; NMR ; Nuclear magnetic resonance ; Peptides</subject><ispartof>RSC advances, 2020-07, Vol.1 (46), p.27331-27335</ispartof><rights>This journal is © The Royal Society of Chemistry.</rights><rights>Copyright Royal Society of Chemistry 2020</rights><rights>This journal is © The Royal Society of Chemistry 2020 The Royal Society of Chemistry</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c369a-968bad34ef75d963a3f699fdf1b8d962466d8c894f13a92ccbe04d62ad00f10e3</citedby><cites>FETCH-LOGICAL-c369a-968bad34ef75d963a3f699fdf1b8d962466d8c894f13a92ccbe04d62ad00f10e3</cites><orcidid>0000-0002-5468-2129 ; 0000-0003-0466-6611</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9055513/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9055513/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27922,27923,53789,53791</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35516938$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dangi, Abha</creatorcontrib><creatorcontrib>Balmik, Abhishek Ankur</creatorcontrib><creatorcontrib>Ghorpade, Archana Kisan</creatorcontrib><creatorcontrib>Gorantla, Nalini Vijay</creatorcontrib><creatorcontrib>Sonawane, Shweta Kishor</creatorcontrib><creatorcontrib>Chinnathambi, Subashchandrabose</creatorcontrib><creatorcontrib>Marelli, Udaya Kiran</creatorcontrib><title>Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6 and AcPHF6</title><title>RSC advances</title><addtitle>RSC Adv</addtitle><description>In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs
via
the interaction of two hexapeptide motifs PHF*
275
VQIINK
280
and PHF
306
VQIVYK
311
as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization.
In the alanine mutant peptides of AcPHF6* and AcPHF6, only the peptides with glutamine to alanine substitution show aggregation akin to that of the parent peptides.</description><subject>Agglomeration</subject><subject>Alanine</subject><subject>Alzheimer's disease</subject><subject>Amino acids</subject><subject>Chemistry</subject><subject>Dichroism</subject><subject>Fluorescence</subject><subject>Glutamine</subject><subject>Morphology</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Peptides</subject><issn>2046-2069</issn><issn>2046-2069</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kc1v1DAQxSMEolXphTvIiAtCCvgjceNLpVWhFKkSqCpna2KPs66ydrATxP73GHZZCgd88YzeT08z86rqKaNvGBXqraUJqOioggfVMaeNrDmV6uG9-qg6zfmOlidbxiV7XB2JtmVSie640jeYvV2w7iGjJVOKE4bs5y2JjsAwJBxg9jEQH8i8RnILC4HNdozexgGDN2SN32HCafYWM1mZz1eXkkCw-_JJ9cjBmPF0_59UXy7f315c1defPny8WF3XRkgFtZJdD1Y06M5aq6QA4aRSzjrWd6XnjZS2M51qHBOguDE90sZKDpZSxyiKk-p85zst_QatwTAnGPWU_AbSVkfw-m8l-LUe4jetaFuOIYrBq71Bil8XzLPe-GxwHCFgXLLmUjLaNZyrgr78B72LSwplPc0b3glBpTgr1OsdZVLMOaE7DMOo_hmdfkdvVr-iWxX4-f3xD-jvoArwbAekbA7qn-yL_uJ_up6sEz8Ab0ipKA</recordid><startdate>20200721</startdate><enddate>20200721</enddate><creator>Dangi, Abha</creator><creator>Balmik, Abhishek Ankur</creator><creator>Ghorpade, Archana Kisan</creator><creator>Gorantla, Nalini Vijay</creator><creator>Sonawane, Shweta Kishor</creator><creator>Chinnathambi, Subashchandrabose</creator><creator>Marelli, Udaya Kiran</creator><general>Royal Society of Chemistry</general><general>The Royal Society of Chemistry</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5468-2129</orcidid><orcidid>https://orcid.org/0000-0003-0466-6611</orcidid></search><sort><creationdate>20200721</creationdate><title>Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6 and AcPHF6</title><author>Dangi, Abha ; Balmik, Abhishek Ankur ; Ghorpade, Archana Kisan ; Gorantla, Nalini Vijay ; Sonawane, Shweta Kishor ; Chinnathambi, Subashchandrabose ; Marelli, Udaya Kiran</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369a-968bad34ef75d963a3f699fdf1b8d962466d8c894f13a92ccbe04d62ad00f10e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Agglomeration</topic><topic>Alanine</topic><topic>Alzheimer's disease</topic><topic>Amino acids</topic><topic>Chemistry</topic><topic>Dichroism</topic><topic>Fluorescence</topic><topic>Glutamine</topic><topic>Morphology</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Peptides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dangi, Abha</creatorcontrib><creatorcontrib>Balmik, Abhishek Ankur</creatorcontrib><creatorcontrib>Ghorpade, Archana Kisan</creatorcontrib><creatorcontrib>Gorantla, Nalini Vijay</creatorcontrib><creatorcontrib>Sonawane, Shweta Kishor</creatorcontrib><creatorcontrib>Chinnathambi, Subashchandrabose</creatorcontrib><creatorcontrib>Marelli, Udaya Kiran</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>RSC advances</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dangi, Abha</au><au>Balmik, Abhishek Ankur</au><au>Ghorpade, Archana Kisan</au><au>Gorantla, Nalini Vijay</au><au>Sonawane, Shweta Kishor</au><au>Chinnathambi, Subashchandrabose</au><au>Marelli, Udaya Kiran</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6 and AcPHF6</atitle><jtitle>RSC advances</jtitle><addtitle>RSC Adv</addtitle><date>2020-07-21</date><risdate>2020</risdate><volume>1</volume><issue>46</issue><spage>27331</spage><epage>27335</epage><pages>27331-27335</pages><issn>2046-2069</issn><eissn>2046-2069</eissn><abstract>In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs
via
the interaction of two hexapeptide motifs PHF*
275
VQIINK
280
and PHF
306
VQIVYK
311
as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization.
In the alanine mutant peptides of AcPHF6* and AcPHF6, only the peptides with glutamine to alanine substitution show aggregation akin to that of the parent peptides.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>35516938</pmid><doi>10.1039/d0ra03809a</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-5468-2129</orcidid><orcidid>https://orcid.org/0000-0003-0466-6611</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2046-2069 |
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| language | eng |
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| source | PubMed Central |
| subjects | Agglomeration Alanine Alzheimer's disease Amino acids Chemistry Dichroism Fluorescence Glutamine Morphology NMR Nuclear magnetic resonance Peptides |
| title | Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6 and AcPHF6 |
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