potential savior. SProC5 (return) cleaves peptide that helps the bacteria resistant to vancomycin.
In the race for current weapons against microbes, vancomycin has long been a weapon of last resort. Unfortunately, more and more bacteria become resistant to the antibiotic. Now, a study hints at a way to extend the life of vancomycin.
Vancomycin works by bonding to a peptide, D-ala-D-ala, that the bacteria use to build their cell wall. This causes the bacteria to absorb much water they burst. But in bacteria resistant to vancomycin, part of this peptide was replaced with D-Ala-D-lac, making the drug ineffective. Gabriela Chiosis chemist at Columbia University and colleague Ivo Gomperts Boneca of Rockefeller University, both in New York, thought they could overcome this problem by splitting D-Ala-D-lac, which would cut leakage cells.
They screened about 300,000 peptides and found one that selectively chopped apart D-Ala-D-Lac. Because peptides are easily chewed by the bacteria, the researchers studied its chemical characteristics and designed a non-peptide compound, SProC5, which mimics the effects of the peptide. SProC5 had no effect on a strain resistant to vancomycin Enterococcus alone, but reduced the amount of vancomycin needed to kill bacteria 8 times, the team reports in the edition 24 August of Science.
SProC5 does not solve the problem of resistance to vancomycin, because even the reduced amount of vancomycin required to kill resistant bacteria would still be toxic to patients, says infectious disease physician Louis Rice Cleveland Veterans Affairs Medical Center in Ohio. Still, "I think it is a very interesting strategy," he said.
Related Sites
US the Food and Drug Administration site on antibiotic resistance
Laboratory Alexander Tomasz
Alliance working for education of antibiotic resistance
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