Double-Stranded DNA Stereoselectively Promotes Aggregation of Amyloid-Like Fibrils and Generates Peptide/DNA Matrices

作者：Yamada Masanori^*; Hara Sachiko; Yamada Tetsuya; Katagiri Fumihiko; Hozumi Kentaro; Nomizu Motoyoshi

来源：Biopolymers, 2014, 102(6): 465-472.

DOI：10.1002/bip.22571

• cell adhesion
• DNA
• laminin
• peptide
• scaffold

An amyloidogenic LAM-L peptide (AASIKVAVSADR, all-L configuration) derived from laminin promoted cell adhesion, neurite outgrowth, and angiogenesis. Here, we prepared novel matrices using double-stranded DNA and the LAM-L peptide. Double-stranded DNA promoted aggregation of amyloid-like fibrils and generated a LAM-L/DNA matrix through electrostatic interactions between the phosphate groups of DNA and the amino groups of LAM-L. This formation of peptide/DNA matrix depends on the Ile-Lys-Val-Ala-Val (IKVAV) sequence in the peptide, since LAM-RM peptide (AASVVIAKSADR), which is scrambled peptide of LAM-L, did not form a matrix with DNA. Further, LAM-D (all-D configuration of LAM-L), which forms amyloid-like fibrils and promotes similar biological activities as LAM-L, did not form amyloid-like fibrils with DNA, suggesting that DNA selectively interacts with the L-configured peptide. Moreover, the LAM-L/DNA matrices showed stronger cell attachment activity compared with LAM-L alone, suggesting the LAM-L/DNA matrices have potential for use as a novel biomaterial in tissue engineering.

• 出版日期2014-11