Structure‐activity study of a laminin α1 chain active peptide segment Ile‐Lys‐Val‐Ala‐Val (IKVAV)

FEBS Letters

Nomizu, Motoyoshi¹  Kim, Woo Hoo¹  Weeks, Benjamin S.²  Weston, Christi A.²  Yamada, Yoshihiko¹  Kleinman, Hynda K.¹ 

[1] Laboratory of Developmental Biology, National Institute of Dental Research, National Institutes of Health, Bldg 30, Rm 427, Bethesda, MD 20892, USA;Department of Biology, Hamilton College, 198 College Hill Rd., Clinton, NY 13323, USA

关键词: Laminin;    IKVAV;    Synthetic peptide;    d-Amino acid;    Cell attachment;    Neurite outgrowth;   

DOI  :  10.1016/0014-5793(95)00475-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The IKVAV sequence, one of the most potent active sites of laminin-1, has been shown to promote cell adhesion, neurite outgrowth, and tumor growth. Here we have determined the structural requirements of the IKVAV sequence for cell attachment and neurite outgrowth using various 12-mer synthetic peptide analogs. All-l- and all-d-IKVAV peptides showed cell attachment and neurite outgrowth activities. In contrast, all-l- and all-d-reverse-sequence peptides were not active. Some of the analogs, in which the lysine and isoleucine residues of the IKVAV peptide were substituted with different amino acids, promoted cell attachment, but none of the analog peptides showed neurite outgrowth activity comparable to that of the IKVAV peptide. These results suggest that the lysine and isoleucine residues are critical for the biological functions of the IKVAV peptide.

【 授权许可】

Unknown