Fibrous Protein Self‐Assembly in Biomimetic Materials

Abstract

Protein self-assembly processes, by which polypeptides interact and independently form multimeric structures, lead to a wide array of different endpoints. Structures formed range from highly ordered molecular crystals to amorphous aggregates. Order arises in the system from a balance between many low-energy processes occurring due to a set of interactions between residues in a chain, between residues in different chains, and between solute and solvent. In Nature, self-assembling protein systems have evolved over millions of years to organize into supramolecular structures, optimized for specific functions, with this propensity determined by the sequence of their constituent amino acids, of which only 20 are encoded in DNA. The structural materials that arise from biological self-assembly can display remarkable mechanical properties, often as a result of hierarchical structure on the nano- and microscales, and much research has been devoted to mimicking and exploiting these properties for a variety of end uses. This work presents a review of a range of studies in which biological functions are effectively reproduced through the design of self-assembling fibrous protein systems.

Self-Assembly of Organic Nanomaterials and Biomaterials: The Bottom-Up Approach for Functional Nanostructures Formation and Advanced Applications

“…The protein self-assembly approaches utilize a number of specific interactions including covalent reactions, hydrogen bond, Van der Waals and electrostatic interactions, receptor-ligand recognitions and metal-ligand coordination. They have been employed for the formation of hierarchical protein nanostructures including, 1D (strings/tubules/nanowires), 2D two-dimensional (nanorings/networks) and 3D (hydrogels and crystalline frameworks) functional nano-assemblies [145]. Their advanced biological functions allow various nanotechnology applications including biomimetic protocells, artificial enzyme, protein-based hydrogel, as well as photosynthesis, drug carriers and imaging nanoplatform [144,145].…”

“…They have been employed for the formation of hierarchical protein nanostructures including, 1D (strings/tubules/nanowires), 2D two-dimensional (nanorings/networks) and 3D (hydrogels and crystalline frameworks) functional nano-assemblies [145]. Their advanced biological functions allow various nanotechnology applications including biomimetic protocells, artificial enzyme, protein-based hydrogel, as well as photosynthesis, drug carriers and imaging nanoplatform [144,145]. Understanding the physico-chemical factors that regulate the peptide and protein self-assembly processes represent the first crucial step for the design and engineering of new building blocks for advanced biotechnology and nanomedicine applications.…”

The Overview of Porous, Bioactive Scaffolds as Instructive Biomaterials for Tissue Regeneration and Their Clinical Translation

“…Polymers derived from natural sources, particularly those derived from extracellular matrix (ECM) are relevant materials for tissue engineering due to their intrinsic bioactivity along with their self-assembling ability [ 93 , 94 ]. For instance, the conformation of fibronectin can orchestrate precisely the delivery of growth factors to cells as shown by Trujillo et al [ 95 ].…”

Fabrication and Mechanical Properties of Engineered Protein‐Based Adhesives and Fibers

“…Besides protein adhesives, ultrastrong and lightweight silk fibers inspired by spider and silkworms have been investigated extensively . Silk fibers are composed of multiple highly modular proteins with repetitive sequences rich in glycine and alanine . Notably, glycine‐rich hydrophilic blocks are responsible for the extendibility of silk fibers, while alanine‐rich hydrophobic blocks are responsible for the high tensile strength .…”