Ile-Lys-Val-Ala-Val (IKVAV)-containing laminin alpha1 chain peptides form amyloid-like fibrils.
The Ile-Lys-Val-Ala-Val (IKVAV) sequence derived from laminin-1 promotes cell adhesion, neurite outgrowth, and tumor growth and metastasis. Here, we examined amyloid formation of an IKVAV-containing peptide (LAM-L: AASIKVAVSADR, mouse laminin alpha1 chain 2097-2108). The LAM-L peptide was stained with Congo red and exhibited fibrils in electron microscopy with a characteristic cross-beta X-ray diffraction pattern. Further, infrared spectra of LAM-L suggested a beta-sheet structure. These results indicate that LAM-L forms amyloid-like fibrils. We also examined amyloid-like fibril formation of LAM-L analogs. The neurite outgrowth activity of the LAM-L analogs was closely related to their amyloid-like fibril formation.
Yamada
Masanori
M
Division of Bioscience, Graduate School of Environmental Earth Science, Hokkaido University, Kita 10 Nishi 5, Kita-ku, Sapporo 060-0810, Japan.
Kadoya
Yuichi
Y
Kasai
Shingo
S
Kato
Kozue
K
Mochizuki
Mayumi
M
Nishi
Norio
N
Watanabe
Nobuhisa
N
Kleinman
Hynda K
HK
Yamada
Yoshihiko
Y
Nomizu
Motoyoshi
M
D000682:Amyloid / Q000737:chemistry*; D003224:Congo Red; D007797:Laminin / Q000737:chemistry*; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D014961:X-Ray Diffraction
D000682:Amyloid; D007797:Laminin; D010446:Peptide Fragments; C083321:isoleucyl-lysyl-valyl-alanyl-valine; C084098:laminin A; D003224:Congo Red