Self-Assembly Toolbox of Tailored Supramolecular Architectures Based on an Amphiphilic Protein Library

A. Schreiber*, L.G. Stühn, M.C. Huber, S.E. Geissinger, A. Rao, S.M. Schiller

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

35 Citations (Scopus)

Abstract

The molecular structuring of complex architectures and the enclosure of space are essential requirements for technical and living systems. Self-assembly of supramolecular structures with desired shape, size, and stability remains challenging since it requires precise regulation of physicochemical and conformational properties of the components. Here a general platform for controlled self-assembly of tailored amphiphilic elastin-like proteins into desired supramolecular protein assemblies ranging from spherical coacervates over molecularly defined twisted fibers to stable unilamellar vesicles is introduced. The described assembly protocols efficiently yield protein membrane–based compartments (PMBC) with adjustable size, stability, and net surface charge. PMBCs demonstrate membrane fusion and phase separation behavior and are able to encapsulate structurally and chemically diverse cargo molecules ranging from small molecules to naturally folded proteins. The ability to engineer tailored supramolecular architectures with defined fusion behavior, tunable properties, and encapsulated cargo paves the road for novel drug delivery systems, the design of artificial cells, and confined catalytic nanofactories.
Original languageEnglish
Article number1900163
JournalSmall
Volume15
Issue number30
DOIs
Publication statusPublished - 2019
Externally publishedYes

Fingerprint

Dive into the research topics of 'Self-Assembly Toolbox of Tailored Supramolecular Architectures Based on an Amphiphilic Protein Library'. Together they form a unique fingerprint.

Cite this