Ile‐Lys‐Val‐Ala‐Val (IKVAV)‐containing laminin α1 chain peptides form amyloid‐like fibrils

FEBS Letters

Nomizu, Motoyoshi³  Mochizuki, Mayumi³  Yamada, Masanori³  Kasai, Shingo³  Watanabe, Nobuhisa¹  Yamada, Yoshihiko²  Kadoya, Yuichi⁴  Kato, Kozue³  Nishi, Norio³  Kleinman, Hynda K.² 

[1] Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan;Craniofacial Developmental Biology and Regeneration Branch, NIDCR, National Institutes of Health, Bethesda, MD 20892-4370, USA;Division of Bioscience, Graduate School of Environmental Earth Science, Hokkaido University, Kita 10 Nishi 5, Kita-ku, Sapporo 060-0810, Japan;Department of Anatomy, Kitasato University School of Medicine, Sagamihara 228-8555, Japan

关键词: Amyloid-like fibril;    Synthetic peptide;    Laminin;    Cell attachment;    Neurite outgrowth;    IR;    infrared;   

DOI  :  10.1016/S0014-5793(02)03393-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α1 chain 2097–2108). The LAM-L peptide was stained with Congo red and exhibited fibrils in electron microscopy with a characteristic cross-β X-ray diffraction pattern. Further, infrared spectra of LAM-L suggested a β-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.

【 授权许可】

Unknown