title: Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides.
abstract: This paper investigates how the properties of multiblock copolypeptides can be tuned by their block architecture, defined by the size and distribution of blocks along the polymer chain. These parameters were explored by the precise, genetically encoded synthesis of recombinant elastin-like polypeptides (ELPs). A family of ELPs was synthesized in which the composition and length were conserved while the block length and distribution were varied, thus creating 11 ELPs with unique block architectures. To our knowledge, these polymers are unprecedented in their intricately and precisely varied architectures. ELPs exhibit lower critical solution temperature (LCST) behavior and micellar self-assembly, both of which impart easily measured physicochemical properties to the copolymers, providing insight into polymer hydrophobicity and self-assembly into higher order structures, as a function of solution temperature. Even subtle variation in block architecture changed the LCST phase behavior and morphology of these ELPs, measured by their temperature-triggered phase transition and nanoscale self-assembly. Size and morphology of polypeptide micelles could be tuned solely by controlling the block architecture, thus demonstrating that when sequence can be precisely controlled, nanoscale self-assembly of polypeptides can be modulated by block architecture.
authors.affiliation: Department of Biomedical Engineering, Duke University , Durham, North Carolina 27708, United States.|Research Triangle Materials Research Science and Engineering Center , Durham, North Carolina 27708, United States.
authors.forename: Sarah R
authors.identifier: 0000-0002-4365-6232
authors.initials: SR
authors.lastname: MacEwan
authors.affiliation: Department of Biomedical Engineering, Duke University , Durham, North Carolina 27708, United States.|Research Triangle Materials Research Science and Engineering Center , Durham, North Carolina 27708, United States.
authors.forename: Isaac
authors.initials: I
authors.lastname: Weitzhandler
authors.affiliation: Stranski-Laboratorium fur Physikalische und Theoretische Chemie, Institut fur Chemie, Technische Universität Berlin , 10623, Berlin, Germany.
authors.forename: Ingo
authors.initials: I
authors.lastname: Hoffmann
authors.affiliation: Research Triangle Materials Research Science and Engineering Center , Durham, North Carolina 27708, United States.|Department of Chemical and Biomolecular Engineering, North Carolina State University , Raleigh, North Carolina 27695, United States.
authors.forename: Jan
authors.identifier: 0000-0002-1633-238X
authors.initials: J
authors.lastname: Genzer
authors.affiliation: Stranski-Laboratorium fur Physikalische und Theoretische Chemie, Institut fur Chemie, Technische Universität Berlin , 10623, Berlin, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Gradzielski
authors.affiliation: Department of Biomedical Engineering, Duke University , Durham, North Carolina 27708, United States.|Research Triangle Materials Research Science and Engineering Center , Durham, North Carolina 27708, United States.
authors.forename: Ashutosh
authors.initials: A
authors.lastname: Chilkoti
mesh_terms: D004549:Elastin / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D010455:Peptides / Q000737:chemistry*; D044367:Phase Transition; D011108:Polymers / Q000737:chemistry*; D044366:Transition Temperature
chemical_list: D008823:Micelles; D010455:Peptides; D011108:Polymers; D004549:Elastin