For the past few decades, ultrashort peptide hydrogels have been at the forefront of biomaterials due to their unique properties like biocompatibility, tunable mechanical properties, and potent antibacterial activity. These ultrashort peptides self-assemble into a hydrogel matrix with nanofibrous networks. In this minireview, we have explored the design and self-assembly of these ultrashort peptide hydrogels by focusing on their antibacterial properties. Cationic and hydrophobic residues are incorporated to engineer the peptides, facilitating interaction with bacterial membranes and leading to membrane disruption and cell death. The hydrogels exhibit broad-spectrum antibacterial activity against both Gram-positive and Gram-negative bacteria. Overall, this minireview highlights the potential of ultrashort peptide hydrogels as versatile and practical antibacterial biomaterials, providing a novel approach to combating bacterial infections and addressing the growing challenge of antibiotic resistance.
Keywords: Amino acid * ultrashort peptide * self-assembly * hydrogel * antimicrobial activity.
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