“…Among the hundreds of amino acids found in nature, 20 amino acids make up all proteins in the human body. − The interactions of these amino acids with water are instrumental for accurate protein folding and maintaining the stability of these complex structures, thus influencing their overall functions. − For example, hydrophobic amino acids, when clustered in the interior of cytoplasmic proteins, may form ligand-binding pockets essential for signaling and enzyme catalysis. − Similarly, hydrophilic amino acids in the interiors of transmembrane proteins are essential for extracellular transport of water and ions, thus maintaining cellular homeostasis. , Moreover, interactions between amino acids and water are advantageous in creating novel peptide-based (macro)molecules including artificial peptide polymers and peptide amphiphiles with unique properties and functionalities. − A combination of both hydrophilic and hydrophobic amino acids in elastin-like polypeptides (ELPs)a class of artificial peptide polymersand their interactions with water is believed to be responsible for their lower critical solution temperature (LCST) behavior. , In the case of peptide amphiphiles (PAs), the sequence of peptides, their concentration, and interactions with water results in self-assembled structures, such as micelles, fibers, rods, and many more, regulated by environmental conditions such as temperature and pH. − Several experimental and computational studies have shown the self-assembly of PAs into micelles and consequently fibers, having micron-sized lengths and nanometer-sized diameters (1–10 nm). ,,− Moreover, self-assembled structures of PAs have shown great promise in biomedical applications like bone regeneration, tissue engineering, gene and drug release, regenerative medicine, etc. ,, Hence, understanding amino acid–water interactions is essential in order to gain insight into the conformations and function of many biomolecules in aqueous solutions.…”