Loading…

Effect of dendrimers on pure acetylcholinesterase activity and structure

The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the...

Full description

Saved in:
Bibliographic Details
Published in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2006, Vol.68 (1), p.56-59
Main Authors: Shcharbin, D., Jokiel, M., Klajnert, B., Bryszewska, M.
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3
cites cdi_FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3
container_end_page 59
container_issue 1
container_start_page 56
container_title Bioelectrochemistry (Amsterdam, Netherlands)
container_volume 68
creator Shcharbin, D.
Jokiel, M.
Klajnert, B.
Bryszewska, M.
description The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the intrinsic fluorescence have shown that the dendrimers changed acetylcholinesterase conformation and the strongest effect was induced by PAMAM G3.5 dendrimer.
doi_str_mv 10.1016/j.bioelechem.2005.04.001
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_885050368</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1567539405000666</els_id><sourcerecordid>885050368</sourcerecordid><originalsourceid>FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3</originalsourceid><addsrcrecordid>eNqFkE1Lw0AQhveg2Fr9C5KTnhpnkuzXUcUvKHjR87LdTOiWNKm7idB_75YWetPTwPC88w4PYxlCjoDifp0vfU8tuRVt8gKA51DlAHjGpsiFnPNSVxN2GeMaABRKfsEmyHVRIi-n7O25acgNWd9kNXV18BsKMeu7bDsGyqyjYde6Vd_6juJAwcb9cvA_fthltquzOITRDYm9YueNbSNdH-eMfb08fz69zRcfr-9PD4u5q6Aa5lrxpuYcKxClbrRFaaGyDsnaZimVtlJJDpJQWyoUldoVlRbIJUokqqmcsbvD3W3ov8f0lNn46KhtbUf9GI1SHDiUQiXy9k9SSIFCFJhAdQBd6GMM1Jht8mDDziCYvWOzNifHZu_YQGWS4xS9OXaMyw3Vp-BRcAIeDwAlJz-egonOU-eo9iF5N3Xv_2_5BTiblKU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67616621</pqid></control><display><type>article</type><title>Effect of dendrimers on pure acetylcholinesterase activity and structure</title><source>Elsevier</source><creator>Shcharbin, D. ; Jokiel, M. ; Klajnert, B. ; Bryszewska, M.</creator><creatorcontrib>Shcharbin, D. ; Jokiel, M. ; Klajnert, B. ; Bryszewska, M.</creatorcontrib><description>The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the intrinsic fluorescence have shown that the dendrimers changed acetylcholinesterase conformation and the strongest effect was induced by PAMAM G3.5 dendrimer.</description><identifier>ISSN: 1567-5394</identifier><identifier>DOI: 10.1016/j.bioelechem.2005.04.001</identifier><identifier>PMID: 15923153</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Acetylcholinesterase ; Acetylcholinesterase - chemistry ; Acetylcholinesterase - metabolism ; Conformation ; Dendrimers - chemistry ; Dendrimers - pharmacology ; Enzyme activity ; Fluorescence ; PAMAM dendrimer ; Protein Conformation - drug effects ; Spectrometry, Fluorescence</subject><ispartof>Bioelectrochemistry (Amsterdam, Netherlands), 2006, Vol.68 (1), p.56-59</ispartof><rights>2005 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3</citedby><cites>FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4021,27921,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15923153$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shcharbin, D.</creatorcontrib><creatorcontrib>Jokiel, M.</creatorcontrib><creatorcontrib>Klajnert, B.</creatorcontrib><creatorcontrib>Bryszewska, M.</creatorcontrib><title>Effect of dendrimers on pure acetylcholinesterase activity and structure</title><title>Bioelectrochemistry (Amsterdam, Netherlands)</title><addtitle>Bioelectrochemistry</addtitle><description>The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the intrinsic fluorescence have shown that the dendrimers changed acetylcholinesterase conformation and the strongest effect was induced by PAMAM G3.5 dendrimer.</description><subject>Acetylcholinesterase</subject><subject>Acetylcholinesterase - chemistry</subject><subject>Acetylcholinesterase - metabolism</subject><subject>Conformation</subject><subject>Dendrimers - chemistry</subject><subject>Dendrimers - pharmacology</subject><subject>Enzyme activity</subject><subject>Fluorescence</subject><subject>PAMAM dendrimer</subject><subject>Protein Conformation - drug effects</subject><subject>Spectrometry, Fluorescence</subject><issn>1567-5394</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkE1Lw0AQhveg2Fr9C5KTnhpnkuzXUcUvKHjR87LdTOiWNKm7idB_75YWetPTwPC88w4PYxlCjoDifp0vfU8tuRVt8gKA51DlAHjGpsiFnPNSVxN2GeMaABRKfsEmyHVRIi-n7O25acgNWd9kNXV18BsKMeu7bDsGyqyjYde6Vd_6juJAwcb9cvA_fthltquzOITRDYm9YueNbSNdH-eMfb08fz69zRcfr-9PD4u5q6Aa5lrxpuYcKxClbrRFaaGyDsnaZimVtlJJDpJQWyoUldoVlRbIJUokqqmcsbvD3W3ov8f0lNn46KhtbUf9GI1SHDiUQiXy9k9SSIFCFJhAdQBd6GMM1Jht8mDDziCYvWOzNifHZu_YQGWS4xS9OXaMyw3Vp-BRcAIeDwAlJz-egonOU-eo9iF5N3Xv_2_5BTiblKU</recordid><startdate>2006</startdate><enddate>2006</enddate><creator>Shcharbin, D.</creator><creator>Jokiel, M.</creator><creator>Klajnert, B.</creator><creator>Bryszewska, M.</creator><general>Elsevier B.V</general><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><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>2006</creationdate><title>Effect of dendrimers on pure acetylcholinesterase activity and structure</title><author>Shcharbin, D. ; Jokiel, M. ; Klajnert, B. ; Bryszewska, M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acetylcholinesterase</topic><topic>Acetylcholinesterase - chemistry</topic><topic>Acetylcholinesterase - metabolism</topic><topic>Conformation</topic><topic>Dendrimers - chemistry</topic><topic>Dendrimers - pharmacology</topic><topic>Enzyme activity</topic><topic>Fluorescence</topic><topic>PAMAM dendrimer</topic><topic>Protein Conformation - drug effects</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shcharbin, D.</creatorcontrib><creatorcontrib>Jokiel, M.</creatorcontrib><creatorcontrib>Klajnert, B.</creatorcontrib><creatorcontrib>Bryszewska, M.</creatorcontrib><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><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Bioelectrochemistry (Amsterdam, Netherlands)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shcharbin, D.</au><au>Jokiel, M.</au><au>Klajnert, B.</au><au>Bryszewska, M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of dendrimers on pure acetylcholinesterase activity and structure</atitle><jtitle>Bioelectrochemistry (Amsterdam, Netherlands)</jtitle><addtitle>Bioelectrochemistry</addtitle><date>2006</date><risdate>2006</risdate><volume>68</volume><issue>1</issue><spage>56</spage><epage>59</epage><pages>56-59</pages><issn>1567-5394</issn><abstract>The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the intrinsic fluorescence have shown that the dendrimers changed acetylcholinesterase conformation and the strongest effect was induced by PAMAM G3.5 dendrimer.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>15923153</pmid><doi>10.1016/j.bioelechem.2005.04.001</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1567-5394
ispartof Bioelectrochemistry (Amsterdam, Netherlands), 2006, Vol.68 (1), p.56-59
issn 1567-5394
language eng
recordid cdi_proquest_miscellaneous_885050368
source Elsevier
subjects Acetylcholinesterase
Acetylcholinesterase - chemistry
Acetylcholinesterase - metabolism
Conformation
Dendrimers - chemistry
Dendrimers - pharmacology
Enzyme activity
Fluorescence
PAMAM dendrimer
Protein Conformation - drug effects
Spectrometry, Fluorescence
title Effect of dendrimers on pure acetylcholinesterase activity and structure
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T10%3A07%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Effect%20of%20dendrimers%20on%20pure%20acetylcholinesterase%20activity%20and%20structure&rft.jtitle=Bioelectrochemistry%20(Amsterdam,%20Netherlands)&rft.au=Shcharbin,%20D.&rft.date=2006&rft.volume=68&rft.issue=1&rft.spage=56&rft.epage=59&rft.pages=56-59&rft.issn=1567-5394&rft_id=info:doi/10.1016/j.bioelechem.2005.04.001&rft_dat=%3Cproquest_cross%3E885050368%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c404t-985fd55140639f9a17a04ac1eaafb789a787507e19ae28e39c2496157171eede3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=67616621&rft_id=info:pmid/15923153&rfr_iscdi=true