Beta‐Sheet‐Forming, Self‐Assembled Peptide Nanomaterials towards Optical, Energy, and Healthcare Applications

Abstract

Peptide self-assembly is an attractive route for the synthesis of intricate organic nanostructures that possess remarkable structural variety and biocompatibility. Recent studies on peptide-based, self-assembled materials have expanded beyond the construction of high-order architectures; they are now reporting new functional materials that have application in the emerging fields such as artificial photosynthesis and rechargeable batteries. Nevertheless, there have been few reviews particularly concentrating on such versatile, emerging applications. Herein, recent advances in the synthesis of self-assembled peptide nanomaterials (e.g., cross β-sheet-based amyloid nanostructures, peptide amphiphiles) are selectively reviewed and their new applications in diverse, interdisciplinary fields are described, ranging from optics and energy storage/conversion to healthcare. The applications of peptide-based self-assembled materials in unconventional fields are also highlighted, such as photoluminescent peptide nanostructures, artificial photosynthetic peptide nanomaterials, and lithium-ion battery components. The relation of such functional materials to the rapidly progressing biomedical applications of peptide self-assembly, which include biosensors/chips and regenerative medicine, are discussed. The combination of strategies shown in these applications would further promote the discovery of novel, functional, small materials.

Natural Polymers for Dye‐Sensitized Solar Cells: Electrolytes and Electrodes

“…Besides polysaccharides, peptides (biologically occurring short chains of amino acid monomers linked by amide bonds) are starting to be considered by the scientific community (38). Proteins and peptides can assist the synthesis of nanostructured inorganic materials in an ecofriendly strategy via a biomineralization process.…”

Self-assembled peptide nanomaterials for biomedical applications: promises and pitfalls

“…24,28 Meanwhile, the peptide sequences with periodically repeated positive and negative charges form the stable structure by ioniccomplementary forces in a checkerboard-like pattern and then assemble typical beta-sheet structures and eventually form a hydrogel network of nanofibers. 13,29 Owing to the combination of ionic force and hydrogen bonds inside the beta-sheet structures, these nanofibers are stable under a wide range of temperatures, pH values, and high concentrations of denaturing chemicals. 26 Since the hydrophobic interactions are not specific, these nanofibers may diffuse to minimize equilibrium energy.…”

“…26 Since the hydrophobic interactions are not specific, these nanofibers may diffuse to minimize equilibrium energy. 13,30 There are different types of ionic-complementary selfassembled peptides ( Figure 2): 1) −+−+−+−+ (eg, peptide RADA16-I: Ac-RADARADARADARADA); 2) −−++−−++ (eg, peptide RADA16-II: Ac-RARADADARARADADA); 3) −−−+++; and 4) −−−−++++. 27,31,32 Among these peptides, the RADA16-I peptide can promote cell growth and tissue regeneration; therefore, it has been commercialized as a product termed PuraMatrix.…”

“…12 At the same time, the external environment, including temperature, pH, ionic strength, and mechanical force, can affect or reverse the self-assembly process. 13 Therefore, based on these properties, scientists can design self-assembled molecules with an "intelligence" to be triggered by the changing environment, such as specific targeting, controlled release, and improved efficacy. 9 To synthesize peptides and their hybrid structures, there are three main methods: solid-phase chemical synthesis, protein engineering, and ring-opening polymerization strategy.…”

Structure-function analysis and characterization of metalloproteins.

“…Thus, the primary structure is a rich source for protein structure and function analysis. while a β-sheet is normally 3-10 residues per strand [45]. Both the α-helix and β-sheet are held together by the hydrogen bond interaction between the amino acid residues.…”