Table 1.
Synthesis and activity of peptides.
|
|
|
Toxicity[b] IC50/μM |
Hemolysis[c] HC50/μM |
MIC[d] μg/mL |
CD[e] |
% Vesicle leakage[f] |
|||
|---|---|---|---|---|---|---|---|---|---|
|
nr. |
Sequence[a] |
HeLa |
HEK 293 |
hRBC |
PAO1 |
A. baumannii |
% α‐helix |
PC |
PG |
|
A1 |
FAKKFFKKFAKFAFK |
8.2±0.5 |
15±0.7 |
>200 |
8 |
8 |
72 |
79 |
43 |
|
A2 |
WFKRILKYLKKLV |
8.4±0.5 |
7.8±0.2 |
60±8 |
8 |
4 |
66 |
78 |
29 |
|
A3 |
WLNALKKILGHLIRH |
8.2±0.8 |
13±0.7 |
30±5 |
16 |
4 |
79 |
100 |
37 |
|
A4 |
KYLKYLVRLVGRLYR |
12±1.4 |
13±1.1 |
61±10 |
16 |
4 |
68 |
96 |
56 |
|
A5 |
WKRIVRIIRWIRKYY |
18±0.2 |
14±0.6 |
93±4 |
>16 |
>16 |
74 |
100 |
46 |
|
A6 |
FAARILRAWFRFLRR |
11±2 |
7.5±0.5 |
23±2 |
>16 |
16 |
75 |
93 |
35 |
|
A7 |
SISRLWHSLLRHLLH |
19±1 |
19±4 |
23±3 |
>16 |
4 |
76 |
100 |
100 |
|
A8 |
KNFKKLMKKVASVL |
>50 |
>50 |
>400 |
8 |
4 |
51 |
16 |
97 |
|
A9 |
SFSKWMGKLKNIFKK |
>50 |
>50 |
>400 |
8 |
8 |
50 |
18 |
32 |
|
A10 |
LLRHCLRRIRDRLV |
>50 |
>50 |
>400 |
16 |
8 |
70 |
56 |
67 |
|
A11 |
KWRSKIKKIMRTFK |
>50 |
>50 |
>400 |
16 |
16 |
46 |
11 |
32 |
|
A12 |
GLLGRLAKLLANS |
>50 |
>50 |
>400 |
16 |
16 |
49 |
1 |
3 |
|
A13 |
VFRQWQKIMRRLVRR |
>50 |
>50 |
>400 |
>16 |
16 |
49 |
2 |
5 |
|
LL–III[g] |
VNWKKILGKIIKVVK |
6.0±0.5 |
15±3 |
>200 |
4‐8 |
4 |
74 |
99 |
72 |
|
B1 |
ANWKKWIGKVIKLVK |
5.5±0.8 |
12±2 |
>200 |
4 |
4 |
70 |
99 |
77 |
|
B2 |
NWKKILGKILDHLAC |
7.0±1.4 |
6.7±0.5 |
322±27 |
>16 |
8 |
68 |
94 |
100 |
|
B3 |
ANWKKILKRLCDI |
22±0.5 |
28±5 |
166±4 |
>16 |
16 |
71 |
62 |
99 |
|
B4 |
NWKKILGKICR |
>50 |
>50 |
>400 |
4 |
4 |
49 |
51 |
99 |
|
B5 |
KNWKKIIKKVVK |
>50 |
>50 |
>400 |
4 |
16 |
35 |
11 |
99 |
|
B6 |
VNVWKKIGRLVKIVK |
>50 |
>50 |
>400 |
8 |
4 |
60 |
50 |
74 |
|
B7 |
NEWKKIKKIIKIVK |
>50 |
>50 |
>400 |
16 |
16 |
49 |
24 |
28 |
|
B8 |
KWRQLGKKIIKVAK |
>50 |
>50 |
>400 |
16 |
16 |
51 |
12 |
99 |
|
B9 |
NWKKIRKLGKVVKKI |
>50 |
>50 |
>400 |
16 |
16 |
40 |
28 |
80 |
|
B10 |
VVNNWKKKIIKVIK |
>50 |
>50 |
>400 |
>16 |
>16 |
48 |
3 |
66 |
|
B11 |
DWHKIGKKVIKVIK |
>50 |
>50 |
>400 |
>16 |
>16 |
53 |
14 |
99 |
|
B12 |
KWNNILGKLGKLAR |
>50 |
>50 |
>400 |
>16 |
>16 |
46 |
4 |
14 |
|
B13 |
NVVGRLGKIVKIVK |
>50 |
>50 |
>400 |
>16 |
>16 |
46 |
1 |
30 |
|
B14 |
NPKVFLKKIIKVVK |
>50 |
>50 |
>400 |
>16 |
>16 |
54 |
0 |
0 |
|
B15 |
ADVWKKVIKVIK |
>50 |
>50 |
>400 |
>16 |
>16 |
42 |
2 |
16 |
|
B16 |
WRGKIGKIIKAVK |
>50 |
>50 |
>400 |
>16 |
>16 |
60 |
16 |
21 |
|
B17 |
NWKKILGRLGEKG |
>50 |
>50 |
>400 |
>16 |
>16 |
26 |
0 |
13 |
|
B18 |
KNWKKIVHDIKNS |
>50 |
>50 |
>400 |
>16 |
>16 |
38 |
1 |
14 |
|
B19 |
NWKKILGKVIDDMKM |
>50 |
>50 |
>400 |
>16 |
>16 |
58 |
16 |
95 |
|
B20 |
DKFSEKLGKIIKIVK |
>50 |
>50 |
>400 |
>16 |
>16 |
62 |
5 |
51 |
|
DLL‐III |
vnwkkilgkiikvvk |
5.0±0.7 |
14.5±2.0 |
>200 |
4 |
2 |
74 |
n.d. |
n.d. |
|
DA1 |
fakkffkkfakfafk |
7.9±0.3 |
15.0±2.3 |
>200 |
4 |
4 |
71 |
n.d. |
n.d. |
|
DB1 |
anwkkwigkviklvk |
6.2±1.1 |
13.1±2.8 |
>200 |
4 |
2 |
71 |
n.d. |
n.d. |
[a] All peptides were synthesized with C‐terminal amidation. [b] IC50 was determined after 72 h incubation at 37 °C in DMEM high glucose medium supplemented with 10 % FBS. [c] HC50 was measured on human red blood cells in 10 mM phosphate buffer saline, pH 7.4, 25 °C. Triton X‐100 was used as a positive control. [d] MIC was determined after incubation for 16–20 h at 37 °C in MH medium. [e] Circular dichroism spectra were measured at concentration 100 μg/mL of peptides in 10 mM phosphate buffer, pH 7.4 in a presence of 5 mM DPC. Percentage of α‐helical structure was calculated by DichroWeb. [f] Fluorescein leakage from phosphatidyl choline (PC) or phosphatidyl glycerol (PG) vesicles was measured in buffer (10 mM TRIS, 107 mM NaCl, pH 7.4) in the presence of 10 μg/mL of peptides. 0.012 % Triton in buffer was used as positive control. [g] Parent peptide lasioglossin III (LL‐III) used for PDGA was synthesized for comparison. n.d.– not determined.