RESUMEN
OBJECTIVE: This study aimed to evaluate the biological characteristics of a human specifically targeted antimi- crobial peptide C16LL-37 against Streptococcus mutans (S. mutans). METHODS: In this study, an antimicrobial peptide LL-37, a peptide derived from CSP(C16) (S. mutans competence stimulating peptide), and recombinant peptide C16LL-37 were synthesized by Fmoc-chemistry-based strategy. The selectivity and antibacterial activity of C16LL-37 were identified by the colony counting method on microbial culture plates. After treatment of C16LL-37 at 32 µmol · L⻹, the morphological changes in S. mutans were observed by using scanning electron microscopy (SEM). In addition, enzyme-linked immunosorbent assay was used to evaluate the hemolytic activity and antibacterial activity of C16LL-37 under different conditions. RESULTS: 1) The minimum inhibitory concentration of C16LL-37 was 16 µmol · L⻹, and the minimum bactericidal concentration was 64 µmol ·L⻹. 2) The survival rate of S. mutans was 3.46% after C16LL-37 treatment at 64 µmo-L⻹ for 30 min, whereas it was 0% at 64 µmol · L⻹ for 60 min. The survival rates of four other kinds of bacteria were more than 60% at any time (P < 0.05). 3) The morphological change in S. mutans was observed after C16LL-37 treatment at 32 µmol · L⻹ by using SEM. S. mutans presented an irregular shape, rough surface, and evident splitting. 4) The hemolysis rate of C16LL-37 (≤ 64 µmol · L⻹) was less than 0.33%. 5) This study showed no significant in- fluence on the antibacterial activity of C16LL-37 under different conditions, such as temperature, pH, salinity, and trypsin at low concentration (P > 0.05). CONCLUSION: C16LL-37 exhibited obvious specificity for S. mutans, strong antibacterial activity, low toxicity, and high stability. Thus, C16LL-37 has good potential in caries research and clinical application.
Asunto(s)
Antiinfecciosos/farmacología , Péptidos Catiónicos Antimicrobianos/farmacología , Streptococcus mutans/efectos de los fármacos , Proteínas Bacterianas , Caries Dental , Ensayo de Inmunoadsorción Enzimática , Humanos , Pruebas de Sensibilidad Microbiana , Microscopía Electrónica de Rastreo , PéptidosRESUMEN
<p><b>OBJECTIVE</b>This study aimed to evaluate the biological characteristics of a human specifically targeted antimi- crobial peptide C16LL-37 against Streptococcus mutans (S. mutans).</p><p><b>METHODS</b>In this study, an antimicrobial peptide LL-37, a peptide derived from CSP(C16) (S. mutans competence stimulating peptide), and recombinant peptide C16LL-37 were synthesized by Fmoc-chemistry-based strategy. The selectivity and antibacterial activity of C16LL-37 were identified by the colony counting method on microbial culture plates. After treatment of C16LL-37 at 32 µmol · L⁻¹, the morphological changes in S. mutans were observed by using scanning electron microscopy (SEM). In addition, enzyme-linked immunosorbent assay was used to evaluate the hemolytic activity and antibacterial activity of C16LL-37 under different conditions.</p><p><b>RESULTS</b>1) The minimum inhibitory concentration of C16LL-37 was 16 µmol · L⁻¹, and the minimum bactericidal concentration was 64 μmol ·L⁻¹. 2) The survival rate of S. mutans was 3.46% after C16LL-37 treatment at 64 µmo-L⁻¹ for 30 min, whereas it was 0% at 64 µmol · L⁻¹ for 60 min. The survival rates of four other kinds of bacteria were more than 60% at any time (P < 0.05). 3) The morphological change in S. mutans was observed after C16LL-37 treatment at 32 µmol · L⁻¹ by using SEM. S. mutans presented an irregular shape, rough surface, and evident splitting. 4) The hemolysis rate of C16LL-37 (≤ 64 µmol · L⁻¹) was less than 0.33%. 5) This study showed no significant in- fluence on the antibacterial activity of C16LL-37 under different conditions, such as temperature, pH, salinity, and trypsin at low concentration (P > 0.05).</p><p><b>CONCLUSION</b>C16LL-37 exhibited obvious specificity for S. mutans, strong antibacterial activity, low toxicity, and high stability. Thus, C16LL-37 has good potential in caries research and clinical application.</p>