Table 1.
Physicochemical properties of Pin2 and Pin2 variants.
Figure 1.
Helical wheel diagrams of Pin2 and Pin2 variants.
Helical wheels were prepared by the software Helical Wheel Projections [56]. The hydrophobic residues are colored in black, hydrophilic and neutral residues are colored in white. A. Pin2, B. Pin2 [G], C. Pin2 [GPG], D. Pin2 [14] and E. Pin2 [17].
Table 2.
Alignment of the sequences of Pin2 [14] and Pin2 [17] with the sequence of other antimicrobial peptides.
Figure 2.
RP-HPLC purification of Pin2 and the variants characterized in this report.
A. Pin2, B. Pin2 [G], C. Pin2 [GPG], D. Pin2 [14] and E. Pin2 [17].
Figure 3.
Circular dichroism of Pin2 and its long and short variants at different concentrations of TFE.
A. CD spectra of Pin2, Pin2 [G] and Pin2 [GPG] at 60% TFE, B. Pin2, C. Pin2 [G], D. Pin2 [GPG], E. Pin2 [14], F. Pin2 [17].
Table 3.
Antimicrobial and hemolytic activities of Pin2 and the Pin2 variants.
Figure 4.
Antimicrobial activity of the Pin2 variants against E. coli ATCC 25922 and S. aureus ATCC 25923.
E. coli antimicrobial activity, A. Pin2 [G], B. Pin2 [GPG], C. Pin2 [14], and D. Pin2 [17]. S. aureus antimicrobial activity, E. Pin2 [G], F. Pin2 [GPG], G. Pin2 [14], and H. Pin2 [17]. The concentration of peptides used was from 0.4 to 25 µM (n = 3).
Table 4.
Antimicrobial activity of Pin2 and the Pin2 variants on two strains of M. tuberculosis.
Figure 5.
Hemolytic activity in human red blood cells.
Data are the average of at least four independent experiments. Error bars represent the standard deviations.