Interaction of amino acid-substituted partial extension peptides of adrenodoxin precursor with artificial membranes and isolated mitochondria.

H. Aoyagi, K. Waki, T. Kato, S. Lee, H. Yamasaki, Shigeki Furuya

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

The N-terminal fragment Met-Ala-Ala-Arg-Leu-Leu-Arg-Val-Ala-Ser-Ala-Ala-Leu-Gly (PA1-14) of the adrenodoxin precursor was previously found to inhibit the import of the precursor into mitochondria. In order to obtain further information on the structure-function relationship, five analogs of PA1-14 ([Leu1]PA1-14 (1), [Leu1,Ala10]PA1-14 (2), [Leu1,Ser4]PA1-14 (3), [Leu1,Arg11]PA1-14 (4) and [Leu1,Ser7,Arg10]PA1-14 (5) were synthesized. The CD study showed that PA1-14 and all analogs were random in an aqueous solution and formed an alpha-helical structure in the solution containing acidic liposomes. Peptides 1 and 2 were found to cause dye leakage from lipid vesicles more strongly than other analogs and PA1-14. All analogs completely inhibited the import of the precursor into mitochondria at a concentration of 30 microM. However, 1 and 2 destroyed the mitochondrial membrane potential. These results indicate that an increase in hydrophobicity by replacement of the Met and Ser residues by Leu and Ala, respectively, participates in the perturbation of the membranes. Furthermore, the requirement for the number and position of the Arg residue was found to be not very strict, although its presence in the extension peptide is essential for the precursor to import into mitochondria.

元の言語英語
ページ(範囲)91-96
ページ数6
ジャーナルPeptide research
5
発行部数2
出版物ステータス出版済み - 1 1 1992

Fingerprint

Adrenodoxin
Artificial Membranes
Mitochondria
Membranes
Amino Acids
Peptides
Mitochondrial Membrane Potential
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Liposomes
Coloring Agents
Lipids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology

これを引用

Interaction of amino acid-substituted partial extension peptides of adrenodoxin precursor with artificial membranes and isolated mitochondria. / Aoyagi, H.; Waki, K.; Kato, T.; Lee, S.; Yamasaki, H.; Furuya, Shigeki.

:: Peptide research, 巻 5, 番号 2, 01.01.1992, p. 91-96.

研究成果: ジャーナルへの寄稿記事

@article{f7c314b9b75d429daf867f7ec9a1d821,
title = "Interaction of amino acid-substituted partial extension peptides of adrenodoxin precursor with artificial membranes and isolated mitochondria.",
abstract = "The N-terminal fragment Met-Ala-Ala-Arg-Leu-Leu-Arg-Val-Ala-Ser-Ala-Ala-Leu-Gly (PA1-14) of the adrenodoxin precursor was previously found to inhibit the import of the precursor into mitochondria. In order to obtain further information on the structure-function relationship, five analogs of PA1-14 ([Leu1]PA1-14 (1), [Leu1,Ala10]PA1-14 (2), [Leu1,Ser4]PA1-14 (3), [Leu1,Arg11]PA1-14 (4) and [Leu1,Ser7,Arg10]PA1-14 (5) were synthesized. The CD study showed that PA1-14 and all analogs were random in an aqueous solution and formed an alpha-helical structure in the solution containing acidic liposomes. Peptides 1 and 2 were found to cause dye leakage from lipid vesicles more strongly than other analogs and PA1-14. All analogs completely inhibited the import of the precursor into mitochondria at a concentration of 30 microM. However, 1 and 2 destroyed the mitochondrial membrane potential. These results indicate that an increase in hydrophobicity by replacement of the Met and Ser residues by Leu and Ala, respectively, participates in the perturbation of the membranes. Furthermore, the requirement for the number and position of the Arg residue was found to be not very strict, although its presence in the extension peptide is essential for the precursor to import into mitochondria.",
author = "H. Aoyagi and K. Waki and T. Kato and S. Lee and H. Yamasaki and Shigeki Furuya",
year = "1992",
month = "1",
day = "1",
language = "English",
volume = "5",
pages = "91--96",
journal = "Peptide Research",
issn = "1040-5704",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Interaction of amino acid-substituted partial extension peptides of adrenodoxin precursor with artificial membranes and isolated mitochondria.

AU - Aoyagi, H.

AU - Waki, K.

AU - Kato, T.

AU - Lee, S.

AU - Yamasaki, H.

AU - Furuya, Shigeki

PY - 1992/1/1

Y1 - 1992/1/1

N2 - The N-terminal fragment Met-Ala-Ala-Arg-Leu-Leu-Arg-Val-Ala-Ser-Ala-Ala-Leu-Gly (PA1-14) of the adrenodoxin precursor was previously found to inhibit the import of the precursor into mitochondria. In order to obtain further information on the structure-function relationship, five analogs of PA1-14 ([Leu1]PA1-14 (1), [Leu1,Ala10]PA1-14 (2), [Leu1,Ser4]PA1-14 (3), [Leu1,Arg11]PA1-14 (4) and [Leu1,Ser7,Arg10]PA1-14 (5) were synthesized. The CD study showed that PA1-14 and all analogs were random in an aqueous solution and formed an alpha-helical structure in the solution containing acidic liposomes. Peptides 1 and 2 were found to cause dye leakage from lipid vesicles more strongly than other analogs and PA1-14. All analogs completely inhibited the import of the precursor into mitochondria at a concentration of 30 microM. However, 1 and 2 destroyed the mitochondrial membrane potential. These results indicate that an increase in hydrophobicity by replacement of the Met and Ser residues by Leu and Ala, respectively, participates in the perturbation of the membranes. Furthermore, the requirement for the number and position of the Arg residue was found to be not very strict, although its presence in the extension peptide is essential for the precursor to import into mitochondria.

AB - The N-terminal fragment Met-Ala-Ala-Arg-Leu-Leu-Arg-Val-Ala-Ser-Ala-Ala-Leu-Gly (PA1-14) of the adrenodoxin precursor was previously found to inhibit the import of the precursor into mitochondria. In order to obtain further information on the structure-function relationship, five analogs of PA1-14 ([Leu1]PA1-14 (1), [Leu1,Ala10]PA1-14 (2), [Leu1,Ser4]PA1-14 (3), [Leu1,Arg11]PA1-14 (4) and [Leu1,Ser7,Arg10]PA1-14 (5) were synthesized. The CD study showed that PA1-14 and all analogs were random in an aqueous solution and formed an alpha-helical structure in the solution containing acidic liposomes. Peptides 1 and 2 were found to cause dye leakage from lipid vesicles more strongly than other analogs and PA1-14. All analogs completely inhibited the import of the precursor into mitochondria at a concentration of 30 microM. However, 1 and 2 destroyed the mitochondrial membrane potential. These results indicate that an increase in hydrophobicity by replacement of the Met and Ser residues by Leu and Ala, respectively, participates in the perturbation of the membranes. Furthermore, the requirement for the number and position of the Arg residue was found to be not very strict, although its presence in the extension peptide is essential for the precursor to import into mitochondria.

UR - http://www.scopus.com/inward/record.url?scp=0026825461&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026825461&partnerID=8YFLogxK

M3 - Article

C2 - 1581642

AN - SCOPUS:0026825461

VL - 5

SP - 91

EP - 96

JO - Peptide Research

JF - Peptide Research

SN - 1040-5704

IS - 2

ER -