| 초록 |
In this study, a HPA3NT3-analogue peptide was designed. In fungal and Gram-negative bacterial cells, HPA3NT3-analogue activity was unchanged or slightly enhanced when compared to the HPA3NT3 peptide. In addition, a two-fold decrease in activity against Gram-positive bacteria was observed. Circular dichroism (CD) spectra revealed that the HPA3NT3-analogue peptide had an unordered structure in buffer and egg yolk L-2-phosphatidyl choline (EYPC), but adapted an α-helical conformation in 50% 2,2,2-trifluoroethanol (TFE) and negatively charged egg yolk L-2- phosphatidyl glycerol (EYPG), while the parent peptide showed an ordered structure in the EYPC. |
