Show simple item record Mackay, JA Callahan, DJ Fitzgerald, KN Chilkoti, A
dc.coverage.spatial United States 2011-06-21T17:22:12Z 2010-11-08
dc.identifier.citation Biomacromolecules, 2010, 11 (11), pp. 2873 - 2879
dc.description.abstract Quantitative models are required to engineer biomaterials with environmentally responsive properties. With this goal in mind, we developed a model that describes the pH-dependent phase behavior of a class of stimulus responsive elastin-like polypeptides (ELPs) that undergo reversible phase separation in response to their solution environment. Under isothermal conditions, charged ELPs can undergo phase separation when their charge is neutralized. Optimization of this behavior has been challenging because the pH at which they phase separate, pHt, depends on their composition, molecular weight, concentration, and temperature. To address this problem, we developed a quantitative model to describe the phase behavior of charged ELPs that uses the Henderson-Hasselbalch relationship to describe the effect of side-chain ionization on the phase-transition temperature of an ELP. The model was validated with pH-responsive ELPs that contained either acidic (Glu) or basic (His) residues. The phase separation of both ELPs fit this model across a range of pH. These results have important implications for applications of pH-responsive ELPs because they provide a quantitative model for the rational design of pH-responsive polypeptides whose transition can be triggered at a specified pH.
dc.format.extent 2873 - 2879
dc.language eng
dc.language.iso en_US en_US
dc.relation.ispartof Biomacromolecules
dc.relation.isversionof 10.1021/bm100571j
dc.subject Elastin
dc.subject Hydrogen-Ion Concentration
dc.subject Models, Molecular
dc.subject Peptides
dc.subject Phase Transition
dc.subject Temperature
dc.title Quantitative model of the phase behavior of recombinant pH-responsive elastin-like polypeptides.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US 2010-11-0 en_US
duke.description.endpage 2879 en_US
duke.description.issue 11 en_US
duke.description.startpage 2873 en_US
duke.description.volume 11 en_US
dc.relation.journal Biomacromolecules en_US
pubs.issue 11
pubs.organisational-group /Duke
pubs.organisational-group /Duke/Pratt School of Engineering
pubs.organisational-group /Duke/Pratt School of Engineering/Biomedical Engineering
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.organisational-group /Duke/Trinity College of Arts & Sciences
pubs.organisational-group /Duke/Trinity College of Arts & Sciences/Chemistry
pubs.publication-status Published
pubs.volume 11
dc.identifier.eissn 1526-4602

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