Interaction of basic extension peptide fragments of adrenodoxin precursor with phospholipid vesicles |
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Authors: | HARUHIKO AOYAGI SANNAMU LEE HIROSHI NAKAMURA NAM GYU PARK TETSUO KATO |
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Affiliation: | HARUHIKO AOYAGI*,SANNAMU LEE,HIROSHI NAKAMURA,NAM GYU PARK,TETSUO KATO |
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Abstract: | 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 α-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. |
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Keywords: | amphiphilic helicity extension peptide dye leakage import inhibition membrane perturbation peptide synthesis |
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