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 alI-D-IKVAV peptides showed cell attachment and neurite outgrowth activities. In contrast, all-Land all-D-reverse-sequence peptides were not active. Some of the analogs, in which the lysine and isolencine 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.

Ni plasma enhanced atomic layer deposition (PE-ALD) using bis(dimethylamino-2-methyl-2-butoxo)nickel [Ni(dmamb) 2 ] as a precursor and NH 3 or H 2 plasma as a reactant was comparatively investigated. PE-ALD Ni using NH 3 plasma showed higher growth rate, lower resistivity, and lower C content than that using H 2 plasma. PE-ALD Ni films were analyzed by X-ray photoelectron spectroscopy (XPS), scanning transmission electron microscopy (STEM), and electron energy loss spectroscopy (EELS). The results showed that the reaction chemistry of ALD using NH 3 plasma was clearly different with that using H 2 , probably due to the effects of NH x radicals. #