Intraglobular structures in multiblock copolymer chains from a Monte Carlo simulation.

TLDR: Self-assembly inMultiblock copolymer chains in implicit nonselective solvents are studied by using a Monte Carlo method, which employs a parallel tempering algorithm, and the relevance of this model to the protein folding is addressed.

Abstract: Multiblock copolymer chains in implicit nonselective solvents are studied by using a Monte Carlo method, which employs a parallel tempering algorithm. Chains consisting of $120 A$ and $120 B$ monomers, arranged in three distinct microarchitectures: $(10\ensuremath{-}10){}_{12}, (6\ensuremath{-}6){}_{20}$, and $(3\ensuremath{-}3){}_{40}$, collapse to globular states upon cooling, as expected. By varying both the reduced temperature ${T}^{*}$ and the compatibility between monomers $\ensuremath{\omega}$, numerous intraglobular structures are obtained: diclusters (handshake, spiral, torus with a core, etc.), triclusters, and $n$ clusters with $ng3$ (lamellar and other), which are reminiscent of the block copolymer nanophases for spherically confined geometries. Phase diagrams for various chains in the (${T}^{*},\ensuremath{\omega}$) space are mapped. The structure factor $S(k)$, for a selected microarchitecture and $\ensuremath{\omega}$, is calculated. Since $S(k)$ can be measured in scattering experiments, it can be used to relate simulation results to an experiment. Self-assembly in those systems is interpreted in terms of competition between minimization of the interfacial area separating different types of monomers and minimization of contacts between chain and solvent. Finally, the relevance of this model to the protein folding is addressed.