WALP peptide

WALP peptides are a class of synthesized, membrane-spanning α-helices composed of tryptophan (W), alanine (A), and leucine (L) amino acids.

They are designed to study properties of proteins in lipid membranes such as orientation, extent of insertion, and hydrophobic mismatch.

The orientations and interactions of these helices directly affect cell signaling and molecular transport across the bilayer.

The hydrophobic environment of the phospholipid tails in turn modulates the position and structure of such domains and thus may influence protein function.

WALPs provide an effective model for studying such interactions because of their systematic design of a core of hydrophobic, alternating alanine and leucine regions.

Following detailed experimental studies by various techniques, the WALP and related peptides have become commonly used model systems in computational biology.

[4] The extent of this tilt is affected up to a certain point by an entropy contribution that arises from the helix's presence in the bilayer and then by more specific helix-lipid interactions.

"Transmembrane Peptides Stabilize Inverted Cubic Phases in a Biphasic Length-Dependent Manner: Implications for Protein-Induced Membrane Fusion".

"Revisiting Hydrophobic Mismatch with Free Energy Simulation Studies of Transmembrane Helix Tilt and Rotation".