Table 2 Circular dichroism data and ΔGif of AR-23 and its analogues.
Peptides | % helixa | ΔGif (kcal/mol)b | |||
|---|---|---|---|---|---|
Water | 30 μM SDS | 50% TFE | 30 μM SDS | 50% TFE | |
Melittin | 12 | 70 | 67 | −8.03 | −7.72 |
RV-23 | 5 | 39 | 33 | −6.11 | −5.56 |
AR-23 | 10 | 57 | 46 | −8.82 | −7.81 |
A(A1R) | 8 | 49 | 38 | −7.45 | −6.44 |
A(A8R) | 7 | 48 | 47 | −7.36 | −7.26 |
A(I17K) | 5 | 43 | 32 | −6.24 | −5.22 |
A(I17R) | 8 | 46 | 33 | −6.69 | −5.5 |
A(A1R, A8R) | 7 | 40 | 34 | −5.98 | −5.43 |
A(A1R, I17K) | 7 | 43 | 28 | −5.6 | −4.22 |
A(A8R, I17K) | 8 | 45 | 30 | −5.78 | −4.4 |
A(A1R, A8R, I17K) | 8 | 45 | 29 | −5.14 | −3.67 |
A(A1R, A8R, I17R) | 6 | 41 | 32 | −4.95 | −4.12 |
- aThe helical content (in percentage) of a peptide was calculated with the following equation: α (%) =
and θf = −39500 × 
, where α is the amount of helix and n is the number of amino acid residues, [θ222] is the experimentally observed absolute mean residue ellipticity at 222 nm. - bCalculations of ΔGif according helix in 30 μM SDS and 50% TFE were performed with MPEx.
and θf = −39500 × 
, where α is the amount of helix and n is the number of amino acid residues, [θ222] is the experimentally observed absolute mean residue ellipticity at 222 nm.