Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding.

The remarkable rise in multi-drug resistant Gram-negative bacterial pathogens is a major concern to the well being of humans as well as susceptible plants. In recent years， diseases associated with inflammation and septicemia have already become a global health issue. Therefore， there is a rising demand for the development of novel "super" antibiotics. In this context， antimicrobial peptides offer an attractive， alternate therapeutic solution to conventional antibiotics.

Antibacterial activity，Antimicrobial peptide，Hemolytic activity，LPS binding，LPS bound conformation，LPS neutralization，Membrane permeabilization，Peptide modifications，trNOESY(Transferred Nuclear Overhauser Effect Spectrosc