Loading…
Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif
In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show th...
Saved in:
| Published in: | Inorganic chemistry 2012-08, Vol.51 (15), p.7960-7962 |
|---|---|
| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | |
|---|---|
| cites | |
| container_end_page | 7962 |
| container_issue | 15 |
| container_start_page | 7960 |
| container_title | Inorganic chemistry |
| container_volume | 51 |
| creator | Ginotra, Yamini P Ramteke, Shefali N Srikanth, Rapole Kulkarni, Prasad P |
| description | In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show that only one His is involved in Cu2+ coordination, which is identified as His6 using mass spectral studies. Novel nickel displacement studies have further supported the proposal that the Cu2+ binding site of Aβ1–16 peptide resembles the ATCUN motif of human serum albumin. |
| doi_str_mv | 10.1021/ic301244x |
| format | article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1032611783</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1032611783</sourcerecordid><originalsourceid>FETCH-LOGICAL-a868-5cdf183da8e826d9c5dfd04a8cbd92e3f35983fece8def25106952d3b4f617f33</originalsourceid><addsrcrecordid>eNo9kMtKw0AUhgdRbK0ufAHJRhAkOpdkOlmW4A1aBVvBjYTJzBlNSZqYyUjd-Q6-iQ_iQ_gkTml1c2585-ecH6FDgs8IpuS8UAwTGkXLLdQnMcVhTPDjNupj7GvCedJDe9bOMcYJi_gu6lEqcBTHoo-eJtLaYNqA6lpZBtPO6QJscA9v4NvuBfyodapzLQS1CUbfX-Tn45NwH1JHT4O0rpoSln7BQpWXxeI5GM3Sh9tgUneF2Uc7RpYWDjZ5gGaXF7P0OhzfXd2ko3EoBRdhrLQhgmkpQFCuExVro3Ekhcp1QoEZFieCGVAgNBjqn-NJTDXLI8PJ0DA2QCdr2aatXx3YLqsKq6As5QJqZzOCGeWEDMUKPdqgLq9AZ01bVLJ9z_4c8cDxGpDKZvPatQt_uFfIVk5n_06zXzbdbwY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1032611783</pqid></control><display><type>article</type><title>Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)</source><creator>Ginotra, Yamini P ; Ramteke, Shefali N ; Srikanth, Rapole ; Kulkarni, Prasad P</creator><creatorcontrib>Ginotra, Yamini P ; Ramteke, Shefali N ; Srikanth, Rapole ; Kulkarni, Prasad P</creatorcontrib><description>In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show that only one His is involved in Cu2+ coordination, which is identified as His6 using mass spectral studies. Novel nickel displacement studies have further supported the proposal that the Cu2+ binding site of Aβ1–16 peptide resembles the ATCUN motif of human serum albumin.</description><identifier>ISSN: 0020-1669</identifier><identifier>EISSN: 1520-510X</identifier><identifier>DOI: 10.1021/ic301244x</identifier><identifier>PMID: 22804558</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Motifs ; Amyloid beta-Peptides - chemistry ; Binding Sites ; Coordination Complexes - chemistry ; Copper - chemistry ; Diethyl Pyrocarbonate ; Histidine - chemistry ; Humans ; Hydrogen-Ion Concentration ; Molecular Conformation ; Nickel ; Peptide Fragments - chemistry ; Protein Binding ; Serum Albumin - chemistry ; Tandem Mass Spectrometry</subject><ispartof>Inorganic chemistry, 2012-08, Vol.51 (15), p.7960-7962</ispartof><rights>Copyright © 2012 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22804558$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ginotra, Yamini P</creatorcontrib><creatorcontrib>Ramteke, Shefali N</creatorcontrib><creatorcontrib>Srikanth, Rapole</creatorcontrib><creatorcontrib>Kulkarni, Prasad P</creatorcontrib><title>Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif</title><title>Inorganic chemistry</title><addtitle>Inorg. Chem</addtitle><description>In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show that only one His is involved in Cu2+ coordination, which is identified as His6 using mass spectral studies. Novel nickel displacement studies have further supported the proposal that the Cu2+ binding site of Aβ1–16 peptide resembles the ATCUN motif of human serum albumin.</description><subject>Amino Acid Motifs</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Binding Sites</subject><subject>Coordination Complexes - chemistry</subject><subject>Copper - chemistry</subject><subject>Diethyl Pyrocarbonate</subject><subject>Histidine - chemistry</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Molecular Conformation</subject><subject>Nickel</subject><subject>Peptide Fragments - chemistry</subject><subject>Protein Binding</subject><subject>Serum Albumin - chemistry</subject><subject>Tandem Mass Spectrometry</subject><issn>0020-1669</issn><issn>1520-510X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNo9kMtKw0AUhgdRbK0ufAHJRhAkOpdkOlmW4A1aBVvBjYTJzBlNSZqYyUjd-Q6-iQ_iQ_gkTml1c2585-ecH6FDgs8IpuS8UAwTGkXLLdQnMcVhTPDjNupj7GvCedJDe9bOMcYJi_gu6lEqcBTHoo-eJtLaYNqA6lpZBtPO6QJscA9v4NvuBfyodapzLQS1CUbfX-Tn45NwH1JHT4O0rpoSln7BQpWXxeI5GM3Sh9tgUneF2Uc7RpYWDjZ5gGaXF7P0OhzfXd2ko3EoBRdhrLQhgmkpQFCuExVro3Ekhcp1QoEZFieCGVAgNBjqn-NJTDXLI8PJ0DA2QCdr2aatXx3YLqsKq6As5QJqZzOCGeWEDMUKPdqgLq9AZ01bVLJ9z_4c8cDxGpDKZvPatQt_uFfIVk5n_06zXzbdbwY</recordid><startdate>20120806</startdate><enddate>20120806</enddate><creator>Ginotra, Yamini P</creator><creator>Ramteke, Shefali N</creator><creator>Srikanth, Rapole</creator><creator>Kulkarni, Prasad P</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20120806</creationdate><title>Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif</title><author>Ginotra, Yamini P ; Ramteke, Shefali N ; Srikanth, Rapole ; Kulkarni, Prasad P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a868-5cdf183da8e826d9c5dfd04a8cbd92e3f35983fece8def25106952d3b4f617f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Motifs</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>Binding Sites</topic><topic>Coordination Complexes - chemistry</topic><topic>Copper - chemistry</topic><topic>Diethyl Pyrocarbonate</topic><topic>Histidine - chemistry</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Molecular Conformation</topic><topic>Nickel</topic><topic>Peptide Fragments - chemistry</topic><topic>Protein Binding</topic><topic>Serum Albumin - chemistry</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ginotra, Yamini P</creatorcontrib><creatorcontrib>Ramteke, Shefali N</creatorcontrib><creatorcontrib>Srikanth, Rapole</creatorcontrib><creatorcontrib>Kulkarni, Prasad P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Inorganic chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ginotra, Yamini P</au><au>Ramteke, Shefali N</au><au>Srikanth, Rapole</au><au>Kulkarni, Prasad P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif</atitle><jtitle>Inorganic chemistry</jtitle><addtitle>Inorg. Chem</addtitle><date>2012-08-06</date><risdate>2012</risdate><volume>51</volume><issue>15</issue><spage>7960</spage><epage>7962</epage><pages>7960-7962</pages><issn>0020-1669</issn><eissn>1520-510X</eissn><abstract>In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show that only one His is involved in Cu2+ coordination, which is identified as His6 using mass spectral studies. Novel nickel displacement studies have further supported the proposal that the Cu2+ binding site of Aβ1–16 peptide resembles the ATCUN motif of human serum albumin.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>22804558</pmid><doi>10.1021/ic301244x</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0020-1669 |
| ispartof | Inorganic chemistry, 2012-08, Vol.51 (15), p.7960-7962 |
| issn | 0020-1669 1520-510X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1032611783 |
| source | American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list) |
| subjects | Amino Acid Motifs Amyloid beta-Peptides - chemistry Binding Sites Coordination Complexes - chemistry Copper - chemistry Diethyl Pyrocarbonate Histidine - chemistry Humans Hydrogen-Ion Concentration Molecular Conformation Nickel Peptide Fragments - chemistry Protein Binding Serum Albumin - chemistry Tandem Mass Spectrometry |
| title | Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T17%3A30%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Mass%20Spectral%20Studies%20Reveal%20the%20Structure%20of%20A%CE%B21%E2%80%9316%E2%80%93Cu2+%20Complex%20Resembling%20ATCUN%20Motif&rft.jtitle=Inorganic%20chemistry&rft.au=Ginotra,%20Yamini%20P&rft.date=2012-08-06&rft.volume=51&rft.issue=15&rft.spage=7960&rft.epage=7962&rft.pages=7960-7962&rft.issn=0020-1669&rft.eissn=1520-510X&rft_id=info:doi/10.1021/ic301244x&rft_dat=%3Cproquest_pubme%3E1032611783%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a868-5cdf183da8e826d9c5dfd04a8cbd92e3f35983fece8def25106952d3b4f617f33%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1032611783&rft_id=info:pmid/22804558&rfr_iscdi=true |