Self-assembly of amino acids toward functional biomaterials

Abstract

Biomolecules, such as proteins and peptides, can be self-assembled. They are widely distributed, easy to obtain, and biocompatible. However, the self-assembly of proteins and peptides has disadvantages, such as difficulty in obtaining high quantities of materials, high cost, polydispersity, and purification limitations. The difficulties in using proteins and peptides as functional materials make it more complicate to arrange assembled nanostructures at both microscopic and macroscopic scales. Amino acids, as the smallest constituent of proteins and the smallest constituent in the bottom-up approach, are the smallest building blocks that can be self-assembled. The self-assembly of single amino acids has the advantages of low synthesis cost, simple modeling, excellent biocompatibility and biodegradability in vivo. In addition, amino acids can be assembled with other components to meet multiple scientific needs. However, using these simple building blocks to design attractive materials remains a challenge due to the simplicity of the amino acids. Most of the review articles about self-assembly focus on large molecules, such as peptides and proteins. The preparation of complicated materials by self-assembly of amino acids has not yet been evaluated. Therefore, it is of great significance to systematically summarize the literature of amino acid self-assembly. This article reviews the recent advances in amino acid self-assembly regarding amino acid self-assembly, functional amino acid self-assembly, amino acid coordination self-assembly, and amino acid regulatory functional molecule self-assembly.

Entropically-Driven Co-assembly of l-Histidine and l-Phenylalanine to Form Supramolecular Materials

“…17−21 Natural aromatic amino acid building blocks, such as L-Phe, L-Tyr, and L-Trp, self-assemble by noncovalent interactions, including hydrogen bonding, aromatic interactions, and van der Waals interactions, to form amyloid-like well-ordered supramolecular assemblies. [1][2][3][4][5][6][7][8][9]22,23 Metal complexes of aromatic amino acids, such as L-Phe with Cu 2+ and Zn 2+ ions, can act as biocatalysts exhibiting high catalytic properties which can be useful in biotechnological, environmental protection, and industrial applications. 24,25 Crystal of Cu 2+ -coordinated L-Phe and D-Phe showed significant magnetic properties that can be used in bioelectronics, spintronics, and various technological applications.…”

Advanced Nanofiber-Based Scaffolds for Achilles Tendon Regenerative Engineering

“…Self-assembled nanofibers, however, have several disadvantages, including low productivity, complex processing, and relatively high cost. Furthermore, self-assembled nanofibers have poor mechanical properties when compared to those prepared using other technologies (Nemati et al, 2019;Ren et al, 2021;Eygeris et al, 2022). Although the phase separation method has advantages such as low cost, ease of manufacture, and simplicity, it also has disadvantages, including lab-scale nanofiber production, long processing time, nanofiber porosity, difficulty to control structural instability, and limitation to polymers suitable for phase separation processes (Dahlin et al, 2011;Kang et al, 2020).…”

Advances in Self‐Assembly of Metabolite Nanostructures: Physiology, Pathology and Nanotechnology

“…Metabolites such as phenylalanine, histidine, asparagine, cysteine, tryptophan and tyrosine form solution-phase β-sheet-like amyloid supramolecular structures (each at 1 mg/mL concentration) as confirmed by Thioflavin T (ThT) binding assay. [43,44] Moreover, the co-assembly of aromatic amino acids such as phenylalanine, tryptophan and histidine (each at 1 mg/mL) with gold nano- [20] (m) A schematic representation of interaction of cells and metabolite amyloid self-assemblies. Reproduced with permission from Ref.…”

“…The self‐assembly of amino acids bears various advantages such as easy modeling, low‐cost synthesis, significant biocompatibility and biodegradability in vivo . Metabolites such as phenylalanine, histidine, asparagine, cysteine, tryptophan and tyrosine form solution‐phase β‐sheet‐like amyloid supramolecular structures (each at 1 mg/mL concentration) as confirmed by Thioflavin T (ThT) binding assay [43,44] . Moreover, the co‐assembly of aromatic amino acids such as phenylalanine, tryptophan and histidine (each at 1 mg/mL) with gold nanoparticles has been utilized to obtain mechanistic insight into increased intermolecular interactions between amino acids and other metabolites which can be used for biomedical applications [45] .…”