Temperature induced complex formation-deformation behavior of collagen model peptides and polyelectrolytes in aqueous solution

Terao, Ken; Kanenaga, Ryoko; Yoshida, Tasuku; Mizuno, Kazunori; Bächinger, Hans Peter

doi:https://doi.org/10.1016/j.polymer.2015.03.013

Temperature induced complex formation-deformation behavior of collagen model peptides and polyelectrolytes in aqueous solution

Terao, Ken; Kanenaga, Ryoko; Yoshida, Tasuku et al.

Polymer, 2015, 64, 8-13

アクセス数:883件（2025-10-25 16:17 集計）

固定URL: https://hdl.handle.net/11094/51740

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タイトル	Temperature induced complex formation-deformation behavior of collagen model peptides and polyelectrolytes in aqueous solution
著者	NRID 1000060334132 1000060334132 ORCID 0000-0001-7363-4491 0000-0001-7363-4491 researchmap permalink kenterao kenterao Scopus Author ID 7101653015 7101653015 著者名 Terao, Ken
	著者名 Kanenaga, Ryoko
	著者名 Yoshida, Tasuku
	著者名 Mizuno, Kazunori
	著者名 Bächinger, Hans Peter
キーワード等	Intermolecular interactions
	Small-angle X-ray scattering
	Sodium carboxymethyl amylose
抄録	Since the triple-helical collagen model peptides with a free N-terminus have three cationic groups at one end, it may have strong interactions with polyelectrolytes. In this study, complex formation behavior was investigated for sodium carboxymethyl amylose (NaCMA) + H-(Pro-Pro-Gly)10-OH (PPG10), a collagen model peptide, in aqueous NaCl with ionic strength of 10 mM and 100 mM by means of small-angle X-ray scattering (SAXS) and circular dichroism at different temperatures. The previously reported [Macromolecules2012, 45, 392–400] sodium polyacrylate (NaPAA) and H-(Gly-Pro-4-(R)-Hyp)9-OH (GPO9) system was also investigated to elucidate complex formation nearby the transition temperature region between triple helix and single coil of the peptide. The complex formed near the melting temperature of the triple helices, confirmed that the triple helical structure is directly related to the complex formation.
出版者	Elsevier
収録物名	Polymer
巻(号)	64
ページ	8-13
刊行年月	2015-05-01
言語	英語
ハンドルURL	https://hdl.handle.net/11094/51740
PISSN	00323861
NCID	AA11537383
関連情報 (isVersionOf)	DOI (出版社版) https://doi.org/10.1016/j.polymer.2015.03.013
アクセス権	open access
権利情報	© 2015 Elsevier Ltd. This manuscript version is made available under the CC-BY-NC-ND 4.0 license. https://creativecommons.org/licenses/by-nc-nd/4.0/
出版タイプ	Accepted Manuscript
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Polymer. 2015, 64, p. 8-13
DC.title	Temperature induced complex formation-deformation behavior of collagen model peptides and polyelectrolytes in aqueous solution
DC.creator	Terao, Ken
	Kanenaga, Ryoko
	Yoshida, Tasuku
	Mizuno, Kazunori
	Bächinger, Hans Peter
DC.publisher	Elsevier
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2015-05-01
DC.identifier	https://doi.org/10.1016/j.polymer.2015.03.013
DC.subject	Intermolecular interactions
	Small-angle X-ray scattering
	Sodium carboxymethyl amylose
DCTERMS.abstract	Since the triple-helical collagen model peptides with a free N-terminus have three cationic groups at one end, it may have strong interactions with polyelectrolytes. In this study, complex formation behavior was investigated for sodium carboxymethyl amylose (NaCMA) + H-(Pro-Pro-Gly)10-OH (PPG10), a collagen model peptide, in aqueous NaCl with ionic strength of 10 mM and 100 mM by means of small-angle X-ray scattering (SAXS) and circular dichroism at different temperatures. The previously reported [Macromolecules2012, 45, 392–400] sodium polyacrylate (NaPAA) and H-(Gly-Pro-4-(R)-Hyp)9-OH (GPO9) system was also investigated to elucidate complex formation nearby the transition temperature region between triple helix and single coil of the peptide. The complex formed near the melting temperature of the triple helices, confirmed that the triple helical structure is directly related to the complex formation.
DC.rights	© 2015 Elsevier Ltd. This manuscript version is made available under the CC-BY-NC-ND 4.0 license. https://creativecommons.org/licenses/by-nc-nd/4.0/
DC.format	51740
citation_title	Temperature induced complex formation-deformation behavior of collagen model peptides and polyelectrolytes in aqueous solution
citation_author	Terao, Ken
	Kanenaga, Ryoko
	Yoshida, Tasuku
	Mizuno, Kazunori
	Bächinger, Hans Peter
citation_publisher	Elsevier
citation_language	英語
citation_date	2015-05-01
citation_journal_title	Polymer
citation_volume	64
citation_firstpage	8
citation_lastpage	13
citation_doi	https://doi.org/10.1016/j.polymer.2015.03.013
citation_public_url	https://hdl.handle.net/11094/51740

Temperature induced complex formation-deformation behavior of collagen model peptides and polyelectrolytes in aqueous solution

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