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Quantitative model of the phase behavior of recombinant pH-responsive elastin-like polypeptides.

dc.contributor.author Mackay, JA
dc.contributor.author Callahan, DJ
dc.contributor.author Fitzgerald, KN
dc.contributor.author Chilkoti, A
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:22:12Z
dc.date.issued 2010-11-08
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20925333
dc.identifier.uri http://hdl.handle.net/10161/4020
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.language eng
dc.language.iso 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
dc.type Journal article
dc.description.version Version of Record
duke.date.pubdate 2010-11-0
duke.description.issue 11
duke.description.volume 11
dc.relation.journal Biomacromolecules
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20925333
pubs.begin-page 2873
pubs.end-page 2879
pubs.issue 11
pubs.organisational-group Biomedical Engineering
pubs.organisational-group Chemistry
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group Pratt School of Engineering
pubs.organisational-group School of Medicine
pubs.organisational-group Trinity College of Arts & Sciences
pubs.publication-status Published
pubs.volume 11
dc.identifier.eissn 1526-4602


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