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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1021/la203518w
|2 doi
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|a pubmed24n0712.xml
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Qin, Si-Yong
|e verfasserin
|4 aut
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|a Morphology transformation via pH-triggered self-assembly of peptides
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|c 2012
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 23.05.2012
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|a Date Revised 25.11.2016
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2011 American Chemical Society
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|a Three flexible peptides (P1: (C(17)H(35)CO-NH-GRGDG)(2)KG; P2: (Fmoc-GRGDG)(2)KG; P3: (CH(3)CO-NH-GRGDG)(2)KG) self-assembled to form a variety of morphologically distinct assemblies at different pHs. P1 formed nanofibers at pH 3, then self-assembled into nanospheres with pH up to 6 and further changed to lamellar structures when the pH value was further increased to 10. P2 aggregated into an entwined network structure at pH 3, and then self-assembled into well-defined nanospheres, lamellar structures, and vesicles via adjusting the pH value. However, P3 did not self-assemble into well-ordered nanostructures, presumably due to the absence of a large hydrophobic group. The varying self-assembly behaviors of the peptides at different pHs are attributed to molecular conformational changes. These self-assembled supramolecular materials might contribute to the development of new peptide-based biomaterials
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Oligopeptides
|2 NLM
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|a arginyl-glycyl-aspartic acid
|2 NLM
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|a 78VO7F77PN
|2 NLM
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|a Xu, Sheng-Sheng
|e verfasserin
|4 aut
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|a Zhuo, Ren-Xi
|e verfasserin
|4 aut
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|a Zhang, Xian-Zheng
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 28(2012), 4 vom: 31. Jan., Seite 2083-90
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|x 1520-5827
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|g volume:28
|g year:2012
|g number:4
|g day:31
|g month:01
|g pages:2083-90
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|u http://dx.doi.org/10.1021/la203518w
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