Design Principles of Self-assembling Peptides and Their Potential Applications

Self-assembling peptides are novel biomaterials, which have recently emerged in the area of nanobiotechnology and nanomedicine. These peptides are capable of self-assembling into stable structures that can withstand extreme conditions of temperature, pH, and the presence of digestive enzymes and denaturation agents. Their biocompatibility and minimal-immunogenicity make them unique biomaterials for tissue engineering and drug and gene delivery. In this article, we discuss the design principles and potential applications of self-assembling peptides. Three major design strategies for self-assembling peptides are currently under intensive research: ionic complementarity, amino acid pairing, and hydrogen bonding complementarity. These designs are based on ionic-complementary, hydrogen-bonding, hydrophobic, and van der Waals’s interactions, among the amino acids in the peptide sequence. These self-assembling peptides have shown great promise for many biomedical applications. Peptide-mediated anticancer drug delivery is the first and one of the most important such applications. These peptides are able to encapsulate hydrophobic anticancer drugs, deliver and release these drugs into the cytoplasm to cause cell death. Small interfere RNA can also be delivered by these peptides to silence particular gene expressions in the cell. Significant other applications of these peptides are in tissue engineering, biosensors, and nanofabrications.