Various types of antibacterial peptides are produced by multicellular organisms for the purpose of defending themselves from pathogenic microbes. Antibacterial peptides have a wide range of inhibitory effects against bacteria and parasites. They also have a great application potential in medicine.
These peptides act as direct antimicrobial agents, modulating the immune response and enhancing wound healing. In addition, they increase chemokine release by immune cells, thereby increasing the ability of the immune system to combat infection.
Antimicrobial peptides are characterized by their ability to penetrate the outer membrane of a bacterial cell and thereby promote uptake of other cationic peptides. They are believed to be internalized by active endocytosis.
The basic structure of a peptide is a backbone with torsion angles. The backbone consists of amino-acid chains that cluster in solution. The overall properties of the peptide are characterized by its charge, hydrophobicity, and chain length.
A number of studies have examined the biophysical properties of membrane-active peptides. These studies use micelle modeling and molecular dynamics simulation.
A new strategy for the development of novel antimicrobial peptides is the use of cationic peptides. These peptides are based on natural templates and have shown synergistic antimicrobial activity with conventional antibiotics. These peptides can be produced in high yields, and are able to cross the outer membrane of Gram-negative bacteria. These peptides also have a low hemolysis rate.
A variety of studies have investigated the use of template-based design methods for peptide design. These methods treat the peptide as a text of individual amino acid letters.