Journal
NANO LETTERS
Volume 14, Issue 11, Pages 6590-6598Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nl503221p
Keywords
Self-assembly; biomaterials; protein polymers; elastin-like polypeptides; cryo-TEM; small-angle neutron scattering
Categories
Funding
- NIH [R01 GM-61232]
- NSF through the Research Triangle MRSEC [NSF-DMR-11-21107]
- National Science Foundation [NSF-DGE-1106401]
- JCNS
- NSF [DMR-1309556, DMR-1120901]
- Direct For Mathematical & Physical Scien [1309556] Funding Source: National Science Foundation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM061232] Funding Source: NIH RePORTER
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Elastin-like polypeptides (ELPs) are a class of biopolymers consisting of the pentameric repeat (VPG alpha G)(n) based on the sequence of mammalian tropoelastin that display a thermally induced soluble-to-insoluble phase transition in aqueous solution. We have discovered a remarkably simple approach to driving the spontaneous self-assembly of high molecular weight ELPs into nanostructures by genetically fusing a short 1.5 kDa (XG(y))(z) assembly domain to one end of the ELP. Classical theories of self-assembly based on the geometric mass balance of hydrophilic and hydrophobic block copolymers suggest that these highly asymmetric polypeptides should form spherical micelles. Surprisingly, when sufficiently hydrophobic amino acids (X) are presented in a periodic sequence such as (FGG)(8) or (YG)(8), these highly asymmetric polypeptides self-assemble into cylindrical micelles whose length can be tuned by the sequence of the morphogenic tag. These nanostructures were characterized by light scattering, tunable resistive pulse sensing, fluorescence spectrophotometry, and thermal turbidimetry, as well as by cryogenic transmission electron microscopy (cryo-TEM) and small-angle neutron scattering (SANS). These short assembly domains provide a facile strategy to control the size, shape, and stability of stimuli responsive polypeptide nanostructures.
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