Antimicrobial Peptide Against Gram Positive With Role Of Amino Acids

Abstract

The study enhance the biocidal activity of singlet oxygen material and the use of surfactants as
transmembrane drug carriers for the protective role of skin bacteria and the importance of competition
between bacteria on the skin. Study of culturable bacteria in human skin was performed to identify the ability
of the skin microbiota about activity against skin pathogens. Propionibacterium acnes, inhibited many grampositive bacteria, including opportunistic skin pathogens such as Staphylococcus epidermidis. Methicillinresistant Staphylococcus aureus (MRSA).
The activity spectrum was generally narrow but highly variable with activity against Actinobacteria,
Proteobacteria, Firmicutes, or specific nasal members of multiple groups of bacteria. Staphylococcal species
and many other Firmicutes species were insensitive to most compounds.
The application of antimicrobial peptides (AMPs) is greatly hampered by their nonspecific toxicity to
mammalian cells, usually associated with their helical structure, hydrophobicity, and charge density,with a
random coil-to-helix transition mechanism has now been introduced into the design of AMPs maintaining
high antibacterial activity. Incorporation of an anionic phosphorylated tyrosine into a cationic polypeptide
distorted the helical conformation of His AMP due to side-chain charge interactions. In addition to reducing
charge density, AMP showed reduced toxicity to mammalian cells. At sites of infection, AMPs are activated
by bacterial phosphatases to restore helical conformation, contributing to their strong membrane-disrupting
ability and potent antibacterial activity. This bacterial activation system is an effective strategy to improve
the therapeutic selectivity of AMPs.