Rachel R Kessler, Sean D Mahoney



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Self-assembly is a process in which molecules autonomously form ordered aggregates held together by non-covalent intermolecular forces. Understanding self-assembly is crucial to nanotechnology and is the missing link between the molecular make-up of biological organisms and the spark that perpetuates them, life. For example, self-assembly offers a powerful way to control the complexity and hierarchy of nanoscale materials. Synthetic efforts that allow a delicate structural design of building units play an important role. However, as can be learned from many cellular processes and functions, co-self-assembly using logically chosen additives should be equally effective in designing self-assembly. Here, by applying this concept, we have assembled cationic surfactant-based self-assembly systems that mimic spider-silk producing protein solutions. Our results reveal that these micelle systems stay as a stable clear solution as long as they are kept sealed and undisturbed. When they are exposed to the air or water, the reactivity of the systems is triggered, which assembles the micelles into liquid crystals having a waxy and flexible nature. The overall assembly very much resembles the assembly process that produces spider silk, where the spidroin-based solutions are kept intact inside a spider’s body, but instantly assemble into liquid crystals once they are extruded into the air. Furthermore, we have identified a clear sign of a meta-stable state and the formation of an aqueous two phase system (ATPS), whose reversible phase transitions are driven by the large changes in entropy of the systems. Though initial, these results demonstrate that it is possible to translate the key features of biological self-assembly into artificial self-assembling systems, and possibly create a new class of soft materials.

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Course Project - Undergraduate

Primary Advisor

Yoon Lee

Primary Advisor's Department



Stander Symposium poster

Surfactant-Based Self-Assembly Systems that Mimic Spider-Silk Producing Protein Sols