Peptide Hall of Fame

ALEXTIDE (aka TrpPocket)

Designer:
Alexander Riemen

Structure:

Sequence:
Ac-RWVWVNGOKILQ-NH2₂

Characteristics:

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.

References:

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.

• Chadtide
• Saratide
• Bobtide
• Alextide