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Ile‐Lys‐Val‐Ala‐Val (IKVAV)‐containing laminin α1 chain peptides form amyloid‐like fibrils
Author(s) -
Yamada Masanori,
Kadoya Yuichi,
Kasai Shingo,
Kato Kozue,
Mochizuki Mayumi,
Nishi Norio,
Watanabe Nobuhisa,
Kleinman Hynda K.,
Yamada Yoshihiko,
Nomizu Motoyoshi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03393-8
Subject(s) - fibril , laminin , chemistry , neurite , amyloid (mycology) , peptide , congo red , biophysics , amyloid fibril , sequence (biology) , microbiology and biotechnology , biochemistry , in vitro , cell , amyloid β , biology , pathology , medicine , inorganic chemistry , disease , organic chemistry , adsorption
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.