Effects of temperature, pH and counterions on the stability of peptide amphiphile nanofiber structures

buir.contributor.authorGüler, Mustafa O.
dc.citation.epage104214en_US
dc.citation.issueNumber106en_US
dc.citation.spage104201en_US
dc.citation.volumeNumber6en_US
dc.contributor.authorOzkan A.D.en_US
dc.contributor.authorTekinay, A. B.en_US
dc.contributor.authorGüler, Mustafa O.en_US
dc.contributor.authorTekin, E. D.en_US
dc.date.accessioned2018-04-12T10:47:58Z
dc.date.available2018-04-12T10:47:58Z
dc.date.issued2016en_US
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)en_US
dc.departmentNanotechnology Research Center (NANOTAM)en_US
dc.description.abstractPeptide amphiphiles are a class of self-assembling molecules that are widely used to form bioactive nanostructures for various applications in bionanomedicine. However, peptide molecules can exhibit distinct behaviors under different conditions, suggesting that environmental variables such as temperature, pH, electrolytes and the presence of biological factors may greatly affect the self-assembly process. In this work, we used united-atom molecular dynamics simulations to understand the effects of three counterions (Na+, Ca2+ at pH 7 and Cl- at pH 2) and temperature change on the stability of the lauryl-VVAGERGD peptide amphiphile self-assembly. This molecule contains a bioactive RGD peptide sequence and has been shown to support cellular adhesion and proliferation in vitro. A 19-layered peptide nanostructure, containing 12 peptide amphiphile molecules per layer, was previously shown to exhibit optimal stability and it was used as the model nanofiber system. Peptide backbone stability was studied under increasing temperatures (300-358 K) using the number of hydrogen bonds and root-mean-square deviations of nanofiber size. At higher temperatures, fiber disintegration was observed to be dependent on the type of counter-ion used for nanofiber formation. Interestingly, rapid heating to higher temperatures could sometimes reestablish the integrity of the nanofiber backbone, possibly by allowing the system to bypass an energy barrier and assuming a more thermodynamically stable configuration. As counterion identity was observed to exhibit remarkable effects on the thermal stability of peptide nanofibers, we suggest that these behaviors should be considered while developing new materials for potential applications.en_US
dc.identifier.doi10.1039/c6ra21261aen_US
dc.identifier.issn2046-2069
dc.identifier.urihttp://hdl.handle.net/11693/36672
dc.language.isoEnglishen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.isversionofhttps://doi.org/10.1039/c6ra21261aen_US
dc.source.titleRSC Advancesen_US
dc.subjectAmphiphilesen_US
dc.subjectHydrogen bondsen_US
dc.subjectIonsen_US
dc.subjectMolecular dynamicsen_US
dc.subjectMoleculesen_US
dc.subjectNanofibersen_US
dc.subjectNanostructuresen_US
dc.subjectpH effectsen_US
dc.subjectPhase equilibriaen_US
dc.subjectPolypeptidesen_US
dc.subjectSelf assemblyen_US
dc.subjectStabilityen_US
dc.subjectTemperatureen_US
dc.subjectThermodynamic stabilityen_US
dc.subjectEffects of temperatureen_US
dc.subjectEnvironmental variablesen_US
dc.subjectIncreasing temperaturesen_US
dc.subjectRoot mean square deviationsen_US
dc.subjectSelf assembling moleculesen_US
dc.subjectSelf assembly processen_US
dc.subjectThermodynamically stableen_US
dc.subjectUnited atom molecular dynamics simulationsen_US
dc.subjectPeptidesen_US
dc.titleEffects of temperature, pH and counterions on the stability of peptide amphiphile nanofiber structuresen_US
dc.typeArticleen_US

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