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.
Highlights
Biomaterials play a crucial role in the treatment of diseases and health care and have been widely used in prostheses and drug delivery devices [1]
The self-assembly of single amino acids has the advantages of low synthesis cost, relatively easy modeling [27], and excellent biocompatibility and biodegradability in vivo [28] compared with the self-assembly of large molecules, such as proteins and peptides
The self-assembly of biomolecules is based on the noncovalent interaction and the bottom-up combination of ordered 3D structures
Summary
Biomaterials play a crucial role in the treatment of diseases and health care and have been widely used in prostheses and drug delivery devices [1]. AdlerAbramovich et al [34] showed for the first time that phenylalanine, a single aromatic amino acid, can form ordered fibrillar assemblies at the nanoscale This component exhibits regular aggregate properties through hydrogen bonding and ion interaction, which are highly similar to those of amyloid components, suggesting that it may be associated with the etiology of amyloid-related diseases. Metal coordination can become a strong interaction due to its near-covalent characteristics compared to the common noncovalent interactions in self-assembly, such as hydrophobic interactions, van der Waals force, hydrogen bonds, ion attraction, and π–π stacking [57]. The amphiphilic amino acid 9-fluorenylmethoxycarbonyl-ʟ-leucine (Fmoc-ʟ-L) and Mn2+ were coordinated to Curcumin is a promising natural antitumor drug, which can inhibit the transformation, proliferation, and migration of tumor cells through various ways, and has anti-angiogenic activity and good biocompatibility [72]. Arginine-modified camptothecin can be combined with anionic cisplatin–polyglutamic acid through electrostatic interaction to construct a co-delivery system
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