Table 2.
Namea | Loop 6 Sequenceb | Hydrophobicc | Negatived | Positivee | Polarf |
---|---|---|---|---|---|
Native | |||||
kB1 | TRNGLPV | 3 | 0 | 1 | 3 |
Residue Mutants | |||||
[Rmut, 16]kB1 | TRRGRPR | 1 | 0 | 4 | 2 |
[Hmut, 16]kB1 | TRHGHPH | 1 | 0 | 4 | 2 |
[Wmut, 16]kB1 | TRWGLPV | 4 | 0 | 1 | 2 |
[Emut, 16]kB1 | TREGEPE | 1 | 3 | 1 | 2 |
[Smut, 16]kB1 | TRSGSPS | 1 | 0 | 1 | 5 |
[Gmut, 16]kB1 | TRGGGPG | 1 | 0 | 1 | 5 |
Grafted Peptides | |||||
[graft1, 16]kB1 | TRGFEWLDWEFGLPV | 8 | 3 | 1 | 3 |
[graft2, 16]kB1 | TRGLDEETGEFGLPV | 5 | 4 | 1 | 5 |
[graft3, 16]kB1 | TRGSFEGYDNGGLPV | 4 | 2 | 1 | 8 |
Chloroalkane (ct) and Alexa Fluor 488 (ax) tagged variants were used to study cellular uptake, but only unlabeled peptides are shown here for brevity. Tags were attached via a lysine at position 16.
Residue differences to the native peptide are highlighted with underlines. Refer to Figure 1 for the rest of the sequence of native kB1 and Table 1 for the rest of the sequence of the kB1 analogues.
Hydrophobic residues: V, P, L, W, F.
Negatively charged residues: D, E.
Positively charged residues: K, R, H.
Polar residues: S, T, Y, N, G.