A breakthrough on how antimicrobial peptides - tiny proteins part of body's immune system kill bacteria may open a new pathway for development of alternatives to antibiotics which have been unsuccessful against superbugs.
It has long been believed that superbugs have no resistance against antimicrobial peptides, but scientists did not understand how they worked, the Age reported.
Lead researcher Associate Professor Michelle Gee, head of the Soft Condensed Matter and Cell Biophysics research group at the University of Melbourne, said it was previously believed that peptides acted like molecular swords - punching holes in membrane holding a bacteria cell together.
This belief was sustained by study that involved tests with peptides and artificial membranes, which essentially, mimic cells without working parts - that routinely left full of holes or pores, and the peptides were seen to gather at the rims.
Gee and her colleagues found peptides produced fewer holes in live bacteria membrane, and main form of invasion took another form entirely.
Instead of punching their way through, peptides wriggle their way through and once disrupted, cell's cytoplasm leaks through membrane and bacteria cell dies, and white blood cells eat up the detritus; the fatal leakage does not come through holes, but through momentary disruptions of wall.
Peptides with their capacity for wriggling and breaking membranes are difficult for bacteria to evolve immunity against.
The research has been published in Scientific Reports.