Peptide Hall of Fame
ALEXTIDE (aka TrpPocket)
Alextide is the derivative of Chadtide and Bobtide in which Glu4 is replaced with a Trp. Alextide was studied as a closer mimic to biological aromatic binding domains of KMe3 in histones. Binding of KMe3 on histones is responsible for gene silencing and activation. This peptide is surprisingly well folded and methylated variants of lysine 9 are even more stable. The trimethylated trp pocket is the most thermal stable still retaining its structure at 80°C.
A.J. Riemen, and M. L. Waters*, "Design of Highly Stabilized β-Hairpin Peptides through Cation-π Interactions of Lysine and N-Methyllysine with an Aromatic Pockets", Biochemistry, 2009, 48, 1525-1531.