Studies of the Minimum Hydrophobicity of α-Helical Peptides Required To Maintain a Stable Transmembrane Association with Phospholipid Bilayer Membranes †

Experimental evidence for predicted tran

Experimental evidence for predicted transmembrane peptide topography: Incorporation of hydrophobic peptide α-helical rods with an N-terminal positive charge having a length comparable to the thickness of lipid bilayers into the membranes

✍ Ryoichi Katakai; Kunihiko Wanikawa; Katsuyuki Saga 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 387 KB

Liposomes consisting of egg yolk phosphatidylcholine and hydrophobic peptides Nps-and C1--+H,-(Met-Met-Leu),-OEt ( n = 6-10) with various polypeptide chain lengths were prepared by the sonication method. The conformation of the peptides incorporated into the liposomes was examined by CD spectroscopy