Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments
The effect of poly(ethylene glycol) PEG crystallization on β-sheet fibril formation is studied for a series of three peptide/PEG conjugates containing fragments modified from the amyloid β peptide, specifically KLVFF, FFKLVFF, and AAKLVFF. These are conjugated to PEG with M n = 3300 g mol−1. It is f...
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Veröffentlicht in: | Langmuir 2008-08, Vol.24 (15), p.8210-8214 |
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description | The effect of poly(ethylene glycol) PEG crystallization on β-sheet fibril formation is studied for a series of three peptide/PEG conjugates containing fragments modified from the amyloid β peptide, specifically KLVFF, FFKLVFF, and AAKLVFF. These are conjugated to PEG with M n = 3300 g mol−1. It is found, via small-angle X-ray scattering, X-ray diffraction, atomic force microscopy, and polarized optical microscopy, that PEG crystallinity in dried samples can disturb fibrillization, in particular cross-β amyloid structure formation, for the conjugate containing the weak fibrillizer KLVFF, whereas this is retained for the conjugates containing the stronger fibrillizers AAKLVFF and FFKLVFF. For these two samples, the alignment of peptide fibrils also drives the orientation of the attached PEG chains. Our results highlight the importance of the antagonistic effects of PEG crystallization and peptide fibril formation in PEG/peptide conjugates. |
doi_str_mv | 10.1021/la8005426 |
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These are conjugated to PEG with M n = 3300 g mol−1. It is found, via small-angle X-ray scattering, X-ray diffraction, atomic force microscopy, and polarized optical microscopy, that PEG crystallinity in dried samples can disturb fibrillization, in particular cross-β amyloid structure formation, for the conjugate containing the weak fibrillizer KLVFF, whereas this is retained for the conjugates containing the stronger fibrillizers AAKLVFF and FFKLVFF. For these two samples, the alignment of peptide fibrils also drives the orientation of the attached PEG chains. Our results highlight the importance of the antagonistic effects of PEG crystallization and peptide fibril formation in PEG/peptide conjugates.</description><identifier>ISSN: 0743-7463</identifier><identifier>EISSN: 1520-5827</identifier><identifier>DOI: 10.1021/la8005426</identifier><identifier>PMID: 18598063</identifier><identifier>CODEN: LANGD5</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Amyloid - chemistry ; Amyloid - ultrastructure ; Chemistry ; Chromatography, High Pressure Liquid ; Colloidal state and disperse state ; Crystallization ; Exact sciences and technology ; General and physical chemistry ; Materials: Nano-and Mesostructured Materials, Polymers, Gels, Liquid Crystals, Composites ; Microscopy, Atomic Force ; Peptide Fragments - chemistry ; Peptide Fragments - ultrastructure ; Polyethylene Glycols - chemistry ; Protein Structure, Secondary ; Spectroscopy, Fourier Transform Infrared ; Surface physical chemistry ; X-Ray Diffraction</subject><ispartof>Langmuir, 2008-08, Vol.24 (15), p.8210-8214</ispartof><rights>Copyright © 2008 American Chemical Society</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a381t-523ff099d6a5677a64a25c7afc94637ea6e85369b852be3fa89c31173d3d478b3</citedby><cites>FETCH-LOGICAL-a381t-523ff099d6a5677a64a25c7afc94637ea6e85369b852be3fa89c31173d3d478b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/la8005426$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/la8005426$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20550782$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18598063$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hamley, Ian W</creatorcontrib><creatorcontrib>Krysmann, Marta J</creatorcontrib><title>Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments</title><title>Langmuir</title><addtitle>Langmuir</addtitle><description>The effect of poly(ethylene glycol) PEG crystallization on β-sheet fibril formation is studied for a series of three peptide/PEG conjugates containing fragments modified from the amyloid β peptide, specifically KLVFF, FFKLVFF, and AAKLVFF. These are conjugated to PEG with M n = 3300 g mol−1. It is found, via small-angle X-ray scattering, X-ray diffraction, atomic force microscopy, and polarized optical microscopy, that PEG crystallinity in dried samples can disturb fibrillization, in particular cross-β amyloid structure formation, for the conjugate containing the weak fibrillizer KLVFF, whereas this is retained for the conjugates containing the stronger fibrillizers AAKLVFF and FFKLVFF. For these two samples, the alignment of peptide fibrils also drives the orientation of the attached PEG chains. Our results highlight the importance of the antagonistic effects of PEG crystallization and peptide fibril formation in PEG/peptide conjugates.</description><subject>Amino Acid Sequence</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - ultrastructure</subject><subject>Chemistry</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Colloidal state and disperse state</subject><subject>Crystallization</subject><subject>Exact sciences and technology</subject><subject>General and physical chemistry</subject><subject>Materials: Nano-and Mesostructured Materials, Polymers, Gels, Liquid Crystals, Composites</subject><subject>Microscopy, Atomic Force</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - ultrastructure</subject><subject>Polyethylene Glycols - chemistry</subject><subject>Protein Structure, Secondary</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Surface physical chemistry</subject><subject>X-Ray Diffraction</subject><issn>0743-7463</issn><issn>1520-5827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0Mtq3DAUBmBRWppp2kVfoHjTQBdudLEuXk7M5EIDmZAphW7EsS2lSmV7Immg7tPHZZzJpiCQQB8_5_wIfST4K8GUnHpQGPOCildoQTjFOVdUvkYLLAuWy0KwI_QuxgeMccmK8i06IoqXCgu2QI8ra02TssFm69VFVoUxJvDe_YXkhj6bTvplsjvjbb6M0XS1H2d7ujbb5FqTVcN28GNnQpyefQLXu_4-W3ajH1ybPavzAPed6VN8j95Y8NF8mO9j9P18taku8-ubi6tqeZ0DUyTlnDJrcVm2AriQEkQBlDcSbFNOC0kDwijORFkrTmvDLKiyYYRI1rK2kKpmx-hkn7sNw-POxKQ7FxvjPfRm2EUtSiaZ4HyCX_awCUOMwVi9Da6DMGqC9b9-9aHfyX6aQ3d1Z9oXORc6gc8zgNiAtwH6xsWDo5hzLBWdXL53Libz5_AP4bcWkkmuN-s7ffbz29ntplL6x0suNFE_DLvQT939Z8Andeec9Q</recordid><startdate>20080805</startdate><enddate>20080805</enddate><creator>Hamley, Ian W</creator><creator>Krysmann, Marta J</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><scope>7X8</scope></search><sort><creationdate>20080805</creationdate><title>Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments</title><author>Hamley, Ian W ; Krysmann, Marta J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-523ff099d6a5677a64a25c7afc94637ea6e85369b852be3fa89c31173d3d478b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - ultrastructure</topic><topic>Chemistry</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Colloidal state and disperse state</topic><topic>Crystallization</topic><topic>Exact sciences and technology</topic><topic>General and physical chemistry</topic><topic>Materials: Nano-and Mesostructured Materials, Polymers, Gels, Liquid Crystals, Composites</topic><topic>Microscopy, Atomic Force</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - ultrastructure</topic><topic>Polyethylene Glycols - chemistry</topic><topic>Protein Structure, Secondary</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Surface physical chemistry</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hamley, Ian W</creatorcontrib><creatorcontrib>Krysmann, Marta J</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</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>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hamley, Ian W</au><au>Krysmann, Marta J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2008-08-05</date><risdate>2008</risdate><volume>24</volume><issue>15</issue><spage>8210</spage><epage>8214</epage><pages>8210-8214</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><coden>LANGD5</coden><abstract>The effect of poly(ethylene glycol) PEG crystallization on β-sheet fibril formation is studied for a series of three peptide/PEG conjugates containing fragments modified from the amyloid β peptide, specifically KLVFF, FFKLVFF, and AAKLVFF. These are conjugated to PEG with M n = 3300 g mol−1. It is found, via small-angle X-ray scattering, X-ray diffraction, atomic force microscopy, and polarized optical microscopy, that PEG crystallinity in dried samples can disturb fibrillization, in particular cross-β amyloid structure formation, for the conjugate containing the weak fibrillizer KLVFF, whereas this is retained for the conjugates containing the stronger fibrillizers AAKLVFF and FFKLVFF. For these two samples, the alignment of peptide fibrils also drives the orientation of the attached PEG chains. Our results highlight the importance of the antagonistic effects of PEG crystallization and peptide fibril formation in PEG/peptide conjugates.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>18598063</pmid><doi>10.1021/la8005426</doi><tpages>5</tpages></addata></record> |
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subjects | Amino Acid Sequence Amyloid - chemistry Amyloid - ultrastructure Chemistry Chromatography, High Pressure Liquid Colloidal state and disperse state Crystallization Exact sciences and technology General and physical chemistry Materials: Nano-and Mesostructured Materials, Polymers, Gels, Liquid Crystals, Composites Microscopy, Atomic Force Peptide Fragments - chemistry Peptide Fragments - ultrastructure Polyethylene Glycols - chemistry Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared Surface physical chemistry X-Ray Diffraction |
title | Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments |
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