Tilted peptides: a motif for membrane destabilization (hypothesis).
Cell life depends on the dynamics of molecular processes: molecule folding, organelle building and transformations involving membrane fusion, protein activation and degradation. To carry out these processes, the hydrophilic/hydrophobic interfaces of amphipathic systems such as membranes and native proteins must be disrupted. In the past decade, protein fragments acting in the disruption of interfaces have been evidenced: they are named the tilted or oblique peptides. Due to a peculiar distribution of hydrophobicity, they can disrupt hydrophobicity interfaces. Tilted peptides should be present in many proteins involved in various stages of cell life. This hypothesis overviews their discovery, describes how they are detected and discusses how they could be involved in dynamic biological processes.
Brasseur
R
R
Centre de Biophysique Moléculaire Numérique, Faculté Universitaire des Sciences Agronomiques de Gembloux, Belgium. brasseur.r@fsagx.ac.be
D000544:Alzheimer Disease / Q000378:metabolism; D020816:Amino Acid Motifs; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008049:Lipase / Q000378:metabolism; D008561:Membrane Fusion; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D021382:Protein Sorting Signals; D014780:Viruses / Q000737:chemistry
D002352:Carrier Proteins; D010446:Peptide Fragments; D021382:Protein Sorting Signals; D008049:Lipase