Loading…
Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate
The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐an...
Saved in:
Published in: | Chembiochem : a European journal of chemical biology 2024-10, Vol.25 (19), p.e202400396-n/a |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | cdi_FETCH-LOGICAL-c2586-d384a4afdfc0bffb7c0ef107c7f41103247f8333ba99e481cb51d7504f49768a3 |
container_end_page | n/a |
container_issue | 19 |
container_start_page | e202400396 |
container_title | Chembiochem : a European journal of chemical biology |
container_volume | 25 |
creator | Hamley, Ian W. Castelletto, Valeria Hermida‐Merino, Daniel Rosenthal, Martin |
description | The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐angle X‐ray scattering (SAXS/WAXS) show that crystallization of PEG is suppressed by αCD, provided that the cyclodextrin content is sufficient. A hexagonal mesophase is formed instead. The αCD threading reduces the conformational flexibility of PEG, and hence suppresses crystallization. These results show that addition of cyclodextrins can be used to tune the crystallization of peptide‐polymer conjugates and potentially other polymer/biomolecular hybrids.
The influence of α‐cyclodextrin (αCD) on crystallization of PEG in an amyloid peptide‐PEG conjugate is investigated by SAXS/WAXS and DSC. The crystallization of PEG is suppressed (with sufficiently high αCD content in the blends) due to complexation with αCD, leading to hexagonal mesophase formation. |
doi_str_mv | 10.1002/cbic.202400396 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_3058637842</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3111740984</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2586-d384a4afdfc0bffb7c0ef107c7f41103247f8333ba99e481cb51d7504f49768a3</originalsourceid><addsrcrecordid>eNqFkM9u1DAQhy1ERUvhyhFZ4sJll_GfjeMjRKWsVNRKwNly7DF4lY2DnagsJx6BZ-yTkNUuReLS04xG33wz-hHygsGSAfA3ro1uyYFLAKGrR-SMSaEXqhLi8bGXnKtT8rSUDQDoSrAn5FTUSq14pc-Ib3auSx5_jDn2d79-r3s_OfT00zQMGUuJqacp0JuLS9rkXRlt18WfdtyPQ05bOn5D-hG7kcae2j02O25wGKNH2qR-M321Iz4jJ8F2BZ8f6zn58v7ic_NhcXV9uW7eXi0cX9XVwotaWmmDDw7aEFrlAAMD5VSQjIHgUoVaCNFarVHWzLUr5tUKZJBaVbUV5-T1wTvk9H3CMpptLA67zvaYpmIEzGeEqiWf0Vf_oZs05X7-zgjGmJKgazlTywPlciolYzBDjlubd4aB2edv9vmb-_znhZdH7dRu0d_jfwOfAX0AbmOHuwd0pnm3bv7J_wAqRJL4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3111740984</pqid></control><display><type>article</type><title>Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate</title><source>Wiley</source><creator>Hamley, Ian W. ; Castelletto, Valeria ; Hermida‐Merino, Daniel ; Rosenthal, Martin</creator><creatorcontrib>Hamley, Ian W. ; Castelletto, Valeria ; Hermida‐Merino, Daniel ; Rosenthal, Martin</creatorcontrib><description>The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐angle X‐ray scattering (SAXS/WAXS) show that crystallization of PEG is suppressed by αCD, provided that the cyclodextrin content is sufficient. A hexagonal mesophase is formed instead. The αCD threading reduces the conformational flexibility of PEG, and hence suppresses crystallization. These results show that addition of cyclodextrins can be used to tune the crystallization of peptide‐polymer conjugates and potentially other polymer/biomolecular hybrids.
The influence of α‐cyclodextrin (αCD) on crystallization of PEG in an amyloid peptide‐PEG conjugate is investigated by SAXS/WAXS and DSC. The crystallization of PEG is suppressed (with sufficiently high αCD content in the blends) due to complexation with αCD, leading to hexagonal mesophase formation.</description><identifier>ISSN: 1439-4227</identifier><identifier>ISSN: 1439-7633</identifier><identifier>EISSN: 1439-7633</identifier><identifier>DOI: 10.1002/cbic.202400396</identifier><identifier>PMID: 38775269</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Addition polymerization ; Calorimetry ; Conjugates ; Crystallization ; Cyclodextrin ; Cyclodextrins ; Differential scanning calorimetry ; Hybrids ; PEG ; Peptide conjugate ; Peptides ; Polyethylene glycol ; Polymers ; Protein structure ; SAXS/WAXS ; β-Amyloid</subject><ispartof>Chembiochem : a European journal of chemical biology, 2024-10, Vol.25 (19), p.e202400396-n/a</ispartof><rights>2024 The Authors. ChemBioChem published by Wiley-VCH GmbH</rights><rights>2024 Wiley‐VCH GmbH.</rights><rights>2024. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2024 The Authors. ChemBioChem published by Wiley-VCH GmbH.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c2586-d384a4afdfc0bffb7c0ef107c7f41103247f8333ba99e481cb51d7504f49768a3</cites><orcidid>0000-0002-4549-0926 ; 0000-0002-3705-0162</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38775269$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hamley, Ian W.</creatorcontrib><creatorcontrib>Castelletto, Valeria</creatorcontrib><creatorcontrib>Hermida‐Merino, Daniel</creatorcontrib><creatorcontrib>Rosenthal, Martin</creatorcontrib><title>Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate</title><title>Chembiochem : a European journal of chemical biology</title><addtitle>Chembiochem</addtitle><description>The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐angle X‐ray scattering (SAXS/WAXS) show that crystallization of PEG is suppressed by αCD, provided that the cyclodextrin content is sufficient. A hexagonal mesophase is formed instead. The αCD threading reduces the conformational flexibility of PEG, and hence suppresses crystallization. These results show that addition of cyclodextrins can be used to tune the crystallization of peptide‐polymer conjugates and potentially other polymer/biomolecular hybrids.
The influence of α‐cyclodextrin (αCD) on crystallization of PEG in an amyloid peptide‐PEG conjugate is investigated by SAXS/WAXS and DSC. The crystallization of PEG is suppressed (with sufficiently high αCD content in the blends) due to complexation with αCD, leading to hexagonal mesophase formation.</description><subject>Addition polymerization</subject><subject>Calorimetry</subject><subject>Conjugates</subject><subject>Crystallization</subject><subject>Cyclodextrin</subject><subject>Cyclodextrins</subject><subject>Differential scanning calorimetry</subject><subject>Hybrids</subject><subject>PEG</subject><subject>Peptide conjugate</subject><subject>Peptides</subject><subject>Polyethylene glycol</subject><subject>Polymers</subject><subject>Protein structure</subject><subject>SAXS/WAXS</subject><subject>β-Amyloid</subject><issn>1439-4227</issn><issn>1439-7633</issn><issn>1439-7633</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNqFkM9u1DAQhy1ERUvhyhFZ4sJll_GfjeMjRKWsVNRKwNly7DF4lY2DnagsJx6BZ-yTkNUuReLS04xG33wz-hHygsGSAfA3ro1uyYFLAKGrR-SMSaEXqhLi8bGXnKtT8rSUDQDoSrAn5FTUSq14pc-Ib3auSx5_jDn2d79-r3s_OfT00zQMGUuJqacp0JuLS9rkXRlt18WfdtyPQ05bOn5D-hG7kcae2j02O25wGKNH2qR-M321Iz4jJ8F2BZ8f6zn58v7ic_NhcXV9uW7eXi0cX9XVwotaWmmDDw7aEFrlAAMD5VSQjIHgUoVaCNFarVHWzLUr5tUKZJBaVbUV5-T1wTvk9H3CMpptLA67zvaYpmIEzGeEqiWf0Vf_oZs05X7-zgjGmJKgazlTywPlciolYzBDjlubd4aB2edv9vmb-_znhZdH7dRu0d_jfwOfAX0AbmOHuwd0pnm3bv7J_wAqRJL4</recordid><startdate>20241001</startdate><enddate>20241001</enddate><creator>Hamley, Ian W.</creator><creator>Castelletto, Valeria</creator><creator>Hermida‐Merino, Daniel</creator><creator>Rosenthal, Martin</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4549-0926</orcidid><orcidid>https://orcid.org/0000-0002-3705-0162</orcidid></search><sort><creationdate>20241001</creationdate><title>Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate</title><author>Hamley, Ian W. ; Castelletto, Valeria ; Hermida‐Merino, Daniel ; Rosenthal, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2586-d384a4afdfc0bffb7c0ef107c7f41103247f8333ba99e481cb51d7504f49768a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Addition polymerization</topic><topic>Calorimetry</topic><topic>Conjugates</topic><topic>Crystallization</topic><topic>Cyclodextrin</topic><topic>Cyclodextrins</topic><topic>Differential scanning calorimetry</topic><topic>Hybrids</topic><topic>PEG</topic><topic>Peptide conjugate</topic><topic>Peptides</topic><topic>Polyethylene glycol</topic><topic>Polymers</topic><topic>Protein structure</topic><topic>SAXS/WAXS</topic><topic>β-Amyloid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hamley, Ian W.</creatorcontrib><creatorcontrib>Castelletto, Valeria</creatorcontrib><creatorcontrib>Hermida‐Merino, Daniel</creatorcontrib><creatorcontrib>Rosenthal, Martin</creatorcontrib><collection>Wiley Open Access</collection><collection>Wiley Online Library Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Chembiochem : a European journal of chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hamley, Ian W.</au><au>Castelletto, Valeria</au><au>Hermida‐Merino, Daniel</au><au>Rosenthal, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate</atitle><jtitle>Chembiochem : a European journal of chemical biology</jtitle><addtitle>Chembiochem</addtitle><date>2024-10-01</date><risdate>2024</risdate><volume>25</volume><issue>19</issue><spage>e202400396</spage><epage>n/a</epage><pages>e202400396-n/a</pages><issn>1439-4227</issn><issn>1439-7633</issn><eissn>1439-7633</eissn><abstract>The influence of alpha‐cyclodextrin (αCD) on PEG crystallization is examined for a peptide‐PEG conjugate, YYKLVFF‐PEG3k comprising an amyloid peptide YYKLVFF linked to PEG with molar mass 3 kg mol−1. Remarkably, differential scanning calorimetry (DSC) and simultaneous synchrotron small‐angle/wide‐angle X‐ray scattering (SAXS/WAXS) show that crystallization of PEG is suppressed by αCD, provided that the cyclodextrin content is sufficient. A hexagonal mesophase is formed instead. The αCD threading reduces the conformational flexibility of PEG, and hence suppresses crystallization. These results show that addition of cyclodextrins can be used to tune the crystallization of peptide‐polymer conjugates and potentially other polymer/biomolecular hybrids.
The influence of α‐cyclodextrin (αCD) on crystallization of PEG in an amyloid peptide‐PEG conjugate is investigated by SAXS/WAXS and DSC. The crystallization of PEG is suppressed (with sufficiently high αCD content in the blends) due to complexation with αCD, leading to hexagonal mesophase formation.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>38775269</pmid><doi>10.1002/cbic.202400396</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-4549-0926</orcidid><orcidid>https://orcid.org/0000-0002-3705-0162</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1439-4227 |
ispartof | Chembiochem : a European journal of chemical biology, 2024-10, Vol.25 (19), p.e202400396-n/a |
issn | 1439-4227 1439-7633 1439-7633 |
language | eng |
recordid | cdi_proquest_miscellaneous_3058637842 |
source | Wiley |
subjects | Addition polymerization Calorimetry Conjugates Crystallization Cyclodextrin Cyclodextrins Differential scanning calorimetry Hybrids PEG Peptide conjugate Peptides Polyethylene glycol Polymers Protein structure SAXS/WAXS β-Amyloid |
title | Cyclodextrin‐Induced Suppression of PEG Crystallization from the Melt in a PEG‐Peptide Conjugate |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T14%3A26%3A56IST&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=Cyclodextrin%E2%80%90Induced%20Suppression%20of%20PEG%20Crystallization%20from%20the%20Melt%20in%20a%20PEG%E2%80%90Peptide%20Conjugate&rft.jtitle=Chembiochem%20:%20a%20European%20journal%20of%20chemical%20biology&rft.au=Hamley,%20Ian%20W.&rft.date=2024-10-01&rft.volume=25&rft.issue=19&rft.spage=e202400396&rft.epage=n/a&rft.pages=e202400396-n/a&rft.issn=1439-4227&rft.eissn=1439-7633&rft_id=info:doi/10.1002/cbic.202400396&rft_dat=%3Cproquest_cross%3E3111740984%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c2586-d384a4afdfc0bffb7c0ef107c7f41103247f8333ba99e481cb51d7504f49768a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=3111740984&rft_id=info:pmid/38775269&rfr_iscdi=true |