Table 1. Peptide designs.
Peptide Name | Sequence1 | MRE222 | Fraction Helix (%) |
Tm (°C) |
---|---|---|---|---|
| ||||
(E2K2)6 | Ac–GEEKKEEKKEEKKEEKKEEKKEEKKGYY–NH2 | 813 | −1 | |
(EK)12 | AC–GEKEKEKEKEKEKEKEKEKEKEKEKGW–NH2 | −8,136 | 22 | |
(KE)12 | AC–GKEKEKEKEKEKEKEKEKEKEKEKEGW–NH2 | −4,180 | 12 | |
| ||||
(E4K4)4 | AC–GEEEEKKKKEEEEKKKKEEEEKKKKEEEEKKKKGW–NH2 | −36,454 | 94 | |
(E4K4)3 | AC–GEEEEKKKKEEEEKKKKEEEEKKKKGW–NH2 | −27,885 | 74 | |
(E4K4)2 | AC–GEEEEKKKKEEEEKKKKGW–NH2 | −23,374 | 65 | |
(E4K4) | AC–GEEEEKKKKGW–NH2 | −4,219 | 14 | |
| ||||
(K4E4)4 | AC–GKKKKEEEEKKKKEEEEKKKKEEEEKKKKEEEEGW–NH2 | −35,479 | 91 | 28 |
(K4E4)3 | AC–GKKKKEEEEKKKKEEEEKKKKEEEEGW–NH2 | −23,493 | 62 | |
(K4E4)2 | AC–GKKKKEEEEKKKKEEEEGW–NH2 | −7,666 | 22 | |
(K4E4) | AC–GKKKKEEEEGW–NH2 | 816 | −1 | |
| ||||
A4(E4K4)3A4 | AC–GAAAAEEEEKKKKEEEEKKKKEEEEKKKKAAAAGW–NH2 | −33,934 | 87 | |
A4(E4K4)2A4 | AC–GAAAAEEEEKKKKEEEEKKKKAAAAGW–NH2 | −27,313 | 72 | |
A4(E4K4)A4 | AC–GAAAAEEEEKKKKAAAAGW–NH2 | −18,885 | 53 | |
| ||||
A4(K4E4)3A4 | AC–GAAAAKKKKEEEEKKKKEEEEKKKKEEEEAAAAGW–NH2 | −38,166 | 98 | 33 |
A4(K4E4)2A4 | AC–GAAAAKKKKEEEEKKKKEEEEAAAAGW–NH2 | −29,687 | 78 | 21 |
A4(K4E4)A4 | AC–GAAAAKKKKEEEEAAAAGW–NH2 | −21,847 | 61 | |
| ||||
A4(E4K4)3 | AC–GAAAAEEEEKKKKEEEEKKKKEEEEKKKKGW–NH2 | −33,288 | 87 | |
(E4K4)3A4 | AC–GEEEEKKKKEEEEKKKKEEEEKKKKAAAAGW–NH2 | −32,668 | 85 | |
| ||||
A4(K4E4)3 | AC–GAAAAKKKKEEEEKKKKEEEEKKKKEEEEGW–NH2 | −35,177 | 91 | 25 |
(K4E4)3A4 | AC–GKKKKEEEEKKKKEEEEKKKKEEEEAAAAGW–NH2 | −32,796 | 85 | 22 |
| ||||
A4(E4K4)A4(E4K4)A4 | AC–GAAAAEEEEKKKKAAAAEEEEKKKKAAAAGW–NH2 | −31,779 | 83 | 24 |
A4(K4E4)A4(K4E4)A4 | AC–GAAAAKKKKEEEEAAAAKKKKEEEEAAAAGW–NH2 | −37,155 | 97 | 29 |
| ||||
(E3K3)4 | AC–GEEEKKKEEEKKKEEEKKKEEEKKKGWW–NH2 | −25,428 | 67 | |
(K3E3)4 | AC–GKKKEEEKKKEEEKKKEEEKKKEEEGWW–NH2 | −12,229 | 33 | |
| ||||
A4(E3K3)4A4 | AC–GAAAAEEEKKKEEEKKKEEEKKKEEEKKKAAAAGWW–NH2 | −31,869 | 82 | 21 |
A4(K3E3)4A4 | AC–GAAAAKKKEEEKKKEEEKKKEEEKKKEEEAAAAGWW–NH2 | −30,287 | 78 | 14 |
Amino acids are represented by standard one-letter codes: A, alanine; E, glutamic acid; G, glycine; and K, lysine. To remove complicating terminal formal charges, and to ameliorate end effects in the helices, the E/K regions in all of the peptides for this study were flanked by glycine residues, and capped with acetyl (Ac) and amide groups (NH2) at their N-and C-termini, respectively. C-terminal tryptophan (W) or tyrosine (Y) residues were included for concentration determination.