Multilayer formation of oriented helical peptides glued by hydrogen bonding

Yoshiko Miura, Guo Chun Xu, Shunsaku Kimura, Shiro Kobayashi, Mitsumasa Iwamoto, Yukio Imanishi, Junzo Umemura

Research output: Contribution to journalConference article

13 Citations (Scopus)

Abstract

Hydrophobic helical peptides having nucleotide base analogues were synthesized, and the helix multilayer was formed by interlayer hydrogen bonds to investigate the surface potential of the multilayer. Hydrophobic helical peptides having a diamino-triazine group at the C-terminal were incubated with the thymine-terminated self-assembled monolayer (SAM). The thin layers of helical peptides were formed with a nearly vertical orientation. The amount of peptide adsorbed on the surface increased with increasing concentration of the peptide solution at preparation, indicating multilayer formation. The numbers of helix layers were 10 and 5 for Boc-(Leu-Aib)8-T (T; 4-N-(aminoethyl)amino-2,6-diamino-1,3,5-triazine) and U-Ala-(Leu-Aib)8-T (U; 6-methyluracil), respectively, when 0.4 mM of peptide solution was used for the preparation. The surface potentials of these multilayers were, respectively, 558 mV and 500 mV. The U-Ala-(Leu-Aib)8-T multilayer generated nearly the same surface potential as the Boc-(Leu-Aib)8-T multilayer, even though the membrane thickness was different. The large positive surface potential should promote electron injection from gold to the thin peptide layer, resulting in saturation of the positive potential generation.

Original languageEnglish
Pages (from-to)59-65
Number of pages7
JournalThin Solid Films
Volume393
Issue number1-2
DOIs
Publication statusPublished - Aug 1 2001
Externally publishedYes
Event4th International Conference on Nano-Molecular Electronics - Kobe, Japan
Duration: Dec 5 2000Dec 7 2000

Fingerprint

Peptides
peptides
Hydrogen bonds
Multilayers
Surface potential
hydrogen
Triazines
helices
vertical orientation
preparation
Electron injection
Thymine
thymine
nucleotides
Self assembled monolayers
Nucleotides
Gold
interlayers
analogs
injection

All Science Journal Classification (ASJC) codes

  • Electronic, Optical and Magnetic Materials
  • Surfaces and Interfaces
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Cite this

Miura, Y., Xu, G. C., Kimura, S., Kobayashi, S., Iwamoto, M., Imanishi, Y., & Umemura, J. (2001). Multilayer formation of oriented helical peptides glued by hydrogen bonding. Thin Solid Films, 393(1-2), 59-65. https://doi.org/10.1016/S0040-6090(01)01097-5

Multilayer formation of oriented helical peptides glued by hydrogen bonding. / Miura, Yoshiko; Xu, Guo Chun; Kimura, Shunsaku; Kobayashi, Shiro; Iwamoto, Mitsumasa; Imanishi, Yukio; Umemura, Junzo.

In: Thin Solid Films, Vol. 393, No. 1-2, 01.08.2001, p. 59-65.

Research output: Contribution to journalConference article

Miura, Y, Xu, GC, Kimura, S, Kobayashi, S, Iwamoto, M, Imanishi, Y & Umemura, J 2001, 'Multilayer formation of oriented helical peptides glued by hydrogen bonding', Thin Solid Films, vol. 393, no. 1-2, pp. 59-65. https://doi.org/10.1016/S0040-6090(01)01097-5
Miura, Yoshiko ; Xu, Guo Chun ; Kimura, Shunsaku ; Kobayashi, Shiro ; Iwamoto, Mitsumasa ; Imanishi, Yukio ; Umemura, Junzo. / Multilayer formation of oriented helical peptides glued by hydrogen bonding. In: Thin Solid Films. 2001 ; Vol. 393, No. 1-2. pp. 59-65.
@article{aadab9e1837445309ae34c4cef88fecf,
title = "Multilayer formation of oriented helical peptides glued by hydrogen bonding",
abstract = "Hydrophobic helical peptides having nucleotide base analogues were synthesized, and the helix multilayer was formed by interlayer hydrogen bonds to investigate the surface potential of the multilayer. Hydrophobic helical peptides having a diamino-triazine group at the C-terminal were incubated with the thymine-terminated self-assembled monolayer (SAM). The thin layers of helical peptides were formed with a nearly vertical orientation. The amount of peptide adsorbed on the surface increased with increasing concentration of the peptide solution at preparation, indicating multilayer formation. The numbers of helix layers were 10 and 5 for Boc-(Leu-Aib)8-T (T; 4-N-(aminoethyl)amino-2,6-diamino-1,3,5-triazine) and U-Ala-(Leu-Aib)8-T (U; 6-methyluracil), respectively, when 0.4 mM of peptide solution was used for the preparation. The surface potentials of these multilayers were, respectively, 558 mV and 500 mV. The U-Ala-(Leu-Aib)8-T multilayer generated nearly the same surface potential as the Boc-(Leu-Aib)8-T multilayer, even though the membrane thickness was different. The large positive surface potential should promote electron injection from gold to the thin peptide layer, resulting in saturation of the positive potential generation.",
author = "Yoshiko Miura and Xu, {Guo Chun} and Shunsaku Kimura and Shiro Kobayashi and Mitsumasa Iwamoto and Yukio Imanishi and Junzo Umemura",
year = "2001",
month = "8",
day = "1",
doi = "10.1016/S0040-6090(01)01097-5",
language = "English",
volume = "393",
pages = "59--65",
journal = "Thin Solid Films",
issn = "0040-6090",
publisher = "Elsevier",
number = "1-2",

}

TY - JOUR

T1 - Multilayer formation of oriented helical peptides glued by hydrogen bonding

AU - Miura, Yoshiko

AU - Xu, Guo Chun

AU - Kimura, Shunsaku

AU - Kobayashi, Shiro

AU - Iwamoto, Mitsumasa

AU - Imanishi, Yukio

AU - Umemura, Junzo

PY - 2001/8/1

Y1 - 2001/8/1

N2 - Hydrophobic helical peptides having nucleotide base analogues were synthesized, and the helix multilayer was formed by interlayer hydrogen bonds to investigate the surface potential of the multilayer. Hydrophobic helical peptides having a diamino-triazine group at the C-terminal were incubated with the thymine-terminated self-assembled monolayer (SAM). The thin layers of helical peptides were formed with a nearly vertical orientation. The amount of peptide adsorbed on the surface increased with increasing concentration of the peptide solution at preparation, indicating multilayer formation. The numbers of helix layers were 10 and 5 for Boc-(Leu-Aib)8-T (T; 4-N-(aminoethyl)amino-2,6-diamino-1,3,5-triazine) and U-Ala-(Leu-Aib)8-T (U; 6-methyluracil), respectively, when 0.4 mM of peptide solution was used for the preparation. The surface potentials of these multilayers were, respectively, 558 mV and 500 mV. The U-Ala-(Leu-Aib)8-T multilayer generated nearly the same surface potential as the Boc-(Leu-Aib)8-T multilayer, even though the membrane thickness was different. The large positive surface potential should promote electron injection from gold to the thin peptide layer, resulting in saturation of the positive potential generation.

AB - Hydrophobic helical peptides having nucleotide base analogues were synthesized, and the helix multilayer was formed by interlayer hydrogen bonds to investigate the surface potential of the multilayer. Hydrophobic helical peptides having a diamino-triazine group at the C-terminal were incubated with the thymine-terminated self-assembled monolayer (SAM). The thin layers of helical peptides were formed with a nearly vertical orientation. The amount of peptide adsorbed on the surface increased with increasing concentration of the peptide solution at preparation, indicating multilayer formation. The numbers of helix layers were 10 and 5 for Boc-(Leu-Aib)8-T (T; 4-N-(aminoethyl)amino-2,6-diamino-1,3,5-triazine) and U-Ala-(Leu-Aib)8-T (U; 6-methyluracil), respectively, when 0.4 mM of peptide solution was used for the preparation. The surface potentials of these multilayers were, respectively, 558 mV and 500 mV. The U-Ala-(Leu-Aib)8-T multilayer generated nearly the same surface potential as the Boc-(Leu-Aib)8-T multilayer, even though the membrane thickness was different. The large positive surface potential should promote electron injection from gold to the thin peptide layer, resulting in saturation of the positive potential generation.

UR - http://www.scopus.com/inward/record.url?scp=0035422359&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035422359&partnerID=8YFLogxK

U2 - 10.1016/S0040-6090(01)01097-5

DO - 10.1016/S0040-6090(01)01097-5

M3 - Conference article

AN - SCOPUS:0035422359

VL - 393

SP - 59

EP - 65

JO - Thin Solid Films

JF - Thin Solid Films

SN - 0040-6090

IS - 1-2

ER -