TABLE 1.
α-Helical basic peptide inhibitors
| Name | Amino acid sequence (species)a | Source | Inhibitory potency (reference) |
|---|---|---|---|
| Bacterial/chloroplast ɛ subunit | MTLNLCVLTPNRSIWNSEVKEIILSTNSGQIGVLPNHAPTATAVDIGILRIRLNDQWLTLALMGGFARIGNNEITILVNDAERGSDIDPQEAQQTLEIAEANLRKAEGKRQKIEANLALRRARTRVEASNTISS (spinach) | Natural regulatory peptide | 1-3 ɛ mol/molc CF1(-ɛ)b (spinach Ca2+-ATPase) (332); ∼0.73 μg/μgc (spinach CF1-Ca2+-ATPase) (284); ∼15 nMc (EF1-ATPase) (372); 100 nMc (EF1-ATPase, rotation rate of 60-nm beads) (282); 10 nMd (EF1-ATPase) (386); 2.1 nMe (Thermosynecoccus ascicula F1, αβγ complex) (212); 94% inhibition at 10 ɛ mol/mol CF1(-ɛ) (spinach Ca2+-ATPase) (289) |
| IF1 | MAVTALAARTWLGVWGVRTMQARGFGSDQSENVDRGAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD (human) | Natural regulatory peptide | 0.25 μMc (bovine heart MF1-ATPase) (143); 1.2 μMc at 21°C and 0.84 μM at 37°C (bovine heart MF1-ATPase) (446); 300 μg/mg proteinc (T. pyriformis SMP-ATPase) (404); 34 μg/mg proteinc (C. asciculate SMP-ATPase) (439); 0.24 μMd (rat liver MF1-ATPase) (229) |
| Melittin | GIGAVLKVLTTGLPALISWIKRKRQQ-NH2 | Apis mellifera (honey bee) | 5 μMc (bovine heart MF1-ATPase) (52); 12 μMc (bovine heart MF1-ATPase) (143) |
| WTf | MLSLRQSIRFFKPATRTLCSSRYLL-NH2 | Subunit IV of yeast cytochrome c oxidase | 16 μMc (bovine heart MF1-ATPase) (52) |
| Δ11,12 | MLSLRQSIRFPATRTLCSSRYLL-NH2 | Synthetic | 29 μMc (bovine heart MF1-ATPase) (52) |
| Syn-A2 | MLSRLSLRLLSRLSLRLLSRYLL-NH2 | Synthetic | 42 nMc (bovine heart MF1-ATPase) (52); 290 nMc (bovine heart MF1-ATPase) (143); 1.7 μMc (Bacillus PS3 F1-ATPase) (143) |
| Syn-C | MLSSLLRLRSLSLLRLRLSRYLL-NH2 | Synthetic | 58 nMc (bovine heart MF1-ATPase) (52); 160 nM (bovine heart MF1-ATPase) (143); 1.6 μMc (Bacillus PS3 F1-ATPase) (143) |
a
Where a species is indicated, sequences vary with species.
b
CF1 without ɛ subunit.
c
I50.
d
Ki.
e
Kd.
f
Leader sequence of subunit IV of yeast cytochrome c oxidase.