J.M. Lehn first introduced the term “supramolecular chemistry” in the literature in 1969 while he was studying the inclusion complexes of Eu^{3 +} with its receptor-molecule cryptands. Lehn defined supramolecular chemistry as “the chemistry of intermolecular bonds”; in a supramolecular system, the same or different chemical compounds are held together by various noncovalent interactions. Amino acids, the building blocks of proteins and peptides, are useful in constructing various supramolecular architectures and forming inclusion complexes with different receptor molecules, including cyclodextrins and calixarenes. Amino acid derivatives also form host-guest inclusion complexes with structurally different receptor molecules, such as chiral crown ethers and cyclodextrines. -Amino-acid-derived lipids become supramolecular receptors through self-assembly, and they host styryl dyes. Many -amino acids form complexes with various types of transition metals, including Pt^{2 +} and lanthanides, leading to the formation of different supramolecular architectures.

Peptides composed of various coded and noncoded amino acid residues self-assemble to form various types of supramolecular architectures, including supramolecular helices and sheets, nanotubes, nanorods, nanovesicles, and nanofibers. The higher-order self-assembly of supramolecular β-sheets or supramolecular helices composed of short synthetic acyclic peptides leads to the formation of amyloid-like fibrils. Synthetic cyclic peptides were used in supramolecular chemistry as molecular scaffolding for artificial receptors, so as to host various chiral and achiral ions and other small neutral substrates. Cyclic peptides also self-assemble like their acyclic counterparts to form supramolecular structures, including hollow nanotubes. Self-assembling cyclic peptides can be served as artificial ion channels, and some of them exhibit potential antimicrobial activities against drug-resistant bacteria.