Aoyagi H, Lee S, Nakamura H, Park N G, Kato T
Laboratory of Biochemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.
Int J Pept Protein Res. 1988 Nov;32(5):406-14. doi: 10.1111/j.1399-3011.1988.tb01275.x.
Two extension peptide fragments PA1-4 and PA17-32, which correspond to the residues 1-14 and 17-32, respectively, of adrenodoxin precursor, were synthesized by the solution method to find a sequence necessary for the import of the precursor into mitochondria. Biological assay showed that PA1-14 inhibited the import of two mitochondrial enzyme precursors, but PA17-32 showed no inhibition, indicating that the N-terminal sequence has important information for import. CD spectra of the peptides demonstrated that PA1-14 formed alpha-helical structure in Tris-HCl buffer (pH 7.4) containing acidic phospholipid liposomes. Furthermore, PA1-14 induced the moderate leakage of carboxyfluorescein from phospholipid vesicles. The relationship between the structure and function of the peptides is discussed.
