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