Type A lantipeptides are cationic antibacterial peptides that may have potential clinical applications in the future. The oral Gram-positive bacterium Streptococcus mutans (S. mutans), strain JH1140 produces the lanti-peptide mutacin 1140. It has previous been shown, that mutacin 1140 has a potent and broad spectrum of activity on several Gram-positive bacteria. The purpose of this study was to investigate the antibacterial po-tential of mutacin 1140, that has undergone a substitution mutation on the first positioned amino acid (Phe1Thr) in the core peptide chain. Mutacin 1140 Phe1Thr was isolated and purified by reverse-phase high-pressure liquid chromatography (RP-HPLC). The fractions from the purified samples, collected from the RP-HPLC, were tested for antibacterial activity by directly spotting them on agar plates coated with Micrococcus luteus (M. luteus). The fractions indicated no antibacterial activity, which directly contradict the results from a previous study. The study had successfully demonstrated that mutacin 1140 Phe1Thr had increased antibacte-rial activity when compared to the wild type mutacin 1140. Thus, the lack of antibacterial activity is indicative of errors that were made in either the synthesis of mutacin 1140 Phe1Thr or in the experimental procedure. For this reason, it was concluded that mutacin 1140 Phe1Thr do have an antibacterial activity against M. lute-us, but that it could not be proven in this study due to some unforeseen errors.
|Uddannelser||Basis - Naturvidenskabelig Bacheloruddannelse, (Bachelor uddannelse) Basis|
|Udgivelsesdato||20 dec. 2016|
- Mutacin 1140
- Type A lantipeptide
- Mutacin 1140 Phe1Thr