TY  - JOUR
AU  - McDaniel, Jonathan R.
AU  - Weitzhandler, Isaac
AU  - Prevost, Sylvain
AU  - Vargo, Kevin B.
AU  - Appavou, Marie-Sousai
AU  - Hammer, Daniel A.
AU  - Gradzielski, Michael
AU  - Chilkoti, Ashutosh
TI  - Noncanonical Self-Assembly of Highly Asymmetric Genetically Encoded Polypeptide Amphiphiles into Cylindrical Micelles
JO  - Nano letters
VL  - 14
IS  - 11
SN  - 1530-6992
CY  - Washington, DC
PB  - ACS Publ.
M1  - FZJ-2014-05401
SP  - 6590–6598
PY  - 2014
AB  - Elastin-like polypeptides (ELPs) are a class of biopolymers consisting of the pentameric repeat (VPGαG)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 (XGy)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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000345723800089
C6  - pmid:25268037
DO  - DOI:10.1021/nl503221p
UR  - https://juser.fz-juelich.de/record/171844
ER  -