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Article: Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA 16-1

TitleTemperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA 16-1
Authors
KeywordsBiophysical and morphological properties
Hemostasis
Peptide RADA16-I
Self-assembling
Issue Date2008
PublisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/6016
Citation
Journal Of Peptide Science, 2008, v. 14 n. 2, p. 152-162 How to Cite?
AbstractIt has been found that the self-assembling peptide RADA 16-I forms a β-sheet structure and self-assembles into nanofibers and scaffolds in favor of cell growth, hemostasis and tissue-injury repair. But its biophysical and morphological properties, especially for its β-sheet and self-assembling properties in heat- and pH-denatured eonditions, remain largely unclear. In order to better understand and design nanobiomaterials, we studied the self-assembly behaviors of RADA16-I using CD and atomic force microscopy (AFM) measurements in various pH and heat-denatured conditions. Here, we report that the peptide, when exposed to pH 1.0 and 4.0, was still able to assume a typical β-sheet structure and self-assemble into long nanofiber, although its β-sheet content was dramatically decreased by 10% in a pH 1.0 solution. However, the peptide, when exposed to pH 13.0, drastically lost its β-sheet structure and assembled into different small-sized globular aggregates. Similarly, the peptide, when heat-denatured from 25 to 70°C, was still able to assume a typieal β-sheet structure with 46% content, but self-assembled into small-sized globular aggregates at much higher temperature. Titration experiments showed that the peptide RADA16-I exists in three types of ionic species: acidic (fully protonated peptide), zwitterionic (electrically neutral peptide carrying partial positive and negative charges) and basic (fully deprotonated peptide) species, called 'super ions'. The unordered structure and β-turn of these 'super ions' via hydrogen or ionic bonds, and heat Brownian motion under the above denatured conditions would directly affect the stability of the β-sheet and nanofibers. These results help us in the design of future nanobiomaterials, such as biosensors, based on β-sheets and environmental changes. These results also help understand the pathogenesis of the β-sheet-mediated neuronal diseases such as Alzheimer's disease and the mechanism of hemostasis. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/67951
ISSN
2015 Impact Factor: 1.951
2015 SCImago Journal Rankings: 0.735
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYe, Zen_HK
dc.contributor.authorZhang, Hen_HK
dc.contributor.authorLuo, Hen_HK
dc.contributor.authorWang, Sen_HK
dc.contributor.authorZhou, Qen_HK
dc.contributor.authorDu, Xen_HK
dc.contributor.authorTang, Cen_HK
dc.contributor.authorChen, Len_HK
dc.contributor.authorLiu, Jen_HK
dc.contributor.authorShi, YKen_HK
dc.contributor.authorZhang, EYen_HK
dc.contributor.authorEllisBehnke, Ren_HK
dc.contributor.authorZhao, Xen_HK
dc.date.accessioned2010-09-06T05:59:45Z-
dc.date.available2010-09-06T05:59:45Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Peptide Science, 2008, v. 14 n. 2, p. 152-162en_HK
dc.identifier.issn1075-2617en_HK
dc.identifier.urihttp://hdl.handle.net/10722/67951-
dc.description.abstractIt has been found that the self-assembling peptide RADA 16-I forms a β-sheet structure and self-assembles into nanofibers and scaffolds in favor of cell growth, hemostasis and tissue-injury repair. But its biophysical and morphological properties, especially for its β-sheet and self-assembling properties in heat- and pH-denatured eonditions, remain largely unclear. In order to better understand and design nanobiomaterials, we studied the self-assembly behaviors of RADA16-I using CD and atomic force microscopy (AFM) measurements in various pH and heat-denatured conditions. Here, we report that the peptide, when exposed to pH 1.0 and 4.0, was still able to assume a typical β-sheet structure and self-assemble into long nanofiber, although its β-sheet content was dramatically decreased by 10% in a pH 1.0 solution. However, the peptide, when exposed to pH 13.0, drastically lost its β-sheet structure and assembled into different small-sized globular aggregates. Similarly, the peptide, when heat-denatured from 25 to 70°C, was still able to assume a typieal β-sheet structure with 46% content, but self-assembled into small-sized globular aggregates at much higher temperature. Titration experiments showed that the peptide RADA16-I exists in three types of ionic species: acidic (fully protonated peptide), zwitterionic (electrically neutral peptide carrying partial positive and negative charges) and basic (fully deprotonated peptide) species, called 'super ions'. The unordered structure and β-turn of these 'super ions' via hydrogen or ionic bonds, and heat Brownian motion under the above denatured conditions would directly affect the stability of the β-sheet and nanofibers. These results help us in the design of future nanobiomaterials, such as biosensors, based on β-sheets and environmental changes. These results also help understand the pathogenesis of the β-sheet-mediated neuronal diseases such as Alzheimer's disease and the mechanism of hemostasis. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/6016en_HK
dc.relation.ispartofJournal of Peptide Scienceen_HK
dc.rightsJournal of Peptide Science. Copyright © John Wiley & Sons Ltd.en_HK
dc.subjectBiophysical and morphological propertiesen_HK
dc.subjectHemostasisen_HK
dc.subjectPeptide RADA16-Ien_HK
dc.subjectSelf-assemblingen_HK
dc.titleTemperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA 16-1en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1075-2617&volume=14&spage=152&epage=162&date=2008&atitle=Temperature+and+pH+Effects+on+Biophysical+and+Morphological+Properties+of+Self-assembling+Peptideen_HK
dc.identifier.emailEllisBehnke, R: rutledg@mit.eduen_HK
dc.identifier.authorityEllisBehnke, R=rp00252en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/psc.988en_HK
dc.identifier.pmid18196533-
dc.identifier.scopuseid_2-s2.0-39649085356en_HK
dc.identifier.hkuros145501en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-39649085356&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume14en_HK
dc.identifier.issue2en_HK
dc.identifier.spage152en_HK
dc.identifier.epage162en_HK
dc.identifier.isiWOS:000253781800006-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridYe, Z=36653302300en_HK
dc.identifier.scopusauthoridZhang, H=23571309500en_HK
dc.identifier.scopusauthoridLuo, H=23571001700en_HK
dc.identifier.scopusauthoridWang, S=26536790600en_HK
dc.identifier.scopusauthoridZhou, Q=25951829000en_HK
dc.identifier.scopusauthoridDu, X=35083418900en_HK
dc.identifier.scopusauthoridTang, C=14623513600en_HK
dc.identifier.scopusauthoridChen, L=22833419200en_HK
dc.identifier.scopusauthoridLiu, J=23570901800en_HK
dc.identifier.scopusauthoridShi, YK=7404963191en_HK
dc.identifier.scopusauthoridZhang, EY=7102686988en_HK
dc.identifier.scopusauthoridEllisBehnke, R=8548055200en_HK
dc.identifier.scopusauthoridZhao, X=7407576427en_HK
dc.identifier.citeulike6601692-

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