Bioinspired Self Assembly of Short Peptides and Their Potential Employment in Biomedical Applications

Abstract

Biomolecules serve as highly attractive foundational components due to their newlineversatility, biocompatibility, biodegradability, and ability to form remarkable supramolecular newlinestructures. Among biomolecules, peptides exhibit exceptional diversity. Extensive research newlinehas been conducted on the self-assembly of peptides, driven by their inherent newlinebiocompatibility, immunogenicity, and ability to create nanostructures with diverse newlinemorphologies, offering promising applications across various domains. Short aromatic newlinepeptides, in particular, have garnered significant interest due to their cost-effective synthesis newlineand chemical modifications when compared to larger bio-macromolecules. Various designer newlinepeptides, including cyclic peptides, amphiphiles, peptide conjugates, and homo-aromatic newlinedipeptides, demonstrate the capability to self-assemble into well-organized structures. The newlinedriving forces behind this self-assembly encompass multiple non-covalent interactions such newlineas aromatic interactions, intermolecular hydrogen bonding, hydrophobic interactions, and newlineinteractions with metal ions. In the realm of natural systems, it is estimated that newlineapproximately one-third of all proteins and enzymes rely on metal ions as cofactors, playing newlinepivotal roles in biological functions by contributing to structural, regulatory, and/or newlineenzymatic processes newline