Monolayer Properties of Hydrophobic α-Helical Peptides Having Various End Groups at the Air/Water Interface

Katsuhiko Fujita; Shunsaku Kimura; Yukio Imanishi; Elmar Rump; Helmut Ringsdorf

doi:10.1021/la00020a038

Monolayer Properties of Hydrophobic α-Helical Peptides Having Various End Groups at the Air/Water Interface

Katsuhiko Fujita, Shunsaku Kimura, Yukio Imanishi, Elmar Rump, Helmut Ringsdorf

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

Abstract

A hydrophobic peptide, Boc-(Ala-Aib)₈-OMe (BA16M), and its end-modified derivatives were synthesized, and the pressure-area (π-A) isotherms of the peptides spread at the air/water interface were studied from the viewpoint of interhelix interactions. All π-A isotherms of the synthetic peptides showed an inflection and weak irregular bumping at a surface areas of about 240 and 230 Å²/molecule, respectively, indicating that the helix axis of the peptide is oriented parallel to the interface. A small mound was observed at around 300 Å²/molecule in the π-a isotherm of BA16M, which was ascribed to the phase transition from a liquid to a solid state. The monolayer of an equimolar mixture of the peptides having an opposite kind of charge in the end group underwent the phase transition in the π-A isotherm, which was not observed with one of the two peptides. The electrostatic interaction between the end groups should stabilize the molecular packing at the interface.

Original language	English
Pages (from-to)	2731-2735
Number of pages	5
Journal	Langmuir
Volume	10
Issue number	8
DOIs	https://doi.org/10.1021/la00020a038
Publication status	Published - Aug 1 1994
Externally published	Yes

All Science Journal Classification (ASJC) codes

Materials Science(all)
Condensed Matter Physics
Surfaces and Interfaces
Spectroscopy
Electrochemistry

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10.1021/la00020a038

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title = "Monolayer Properties of Hydrophobic α-Helical Peptides Having Various End Groups at the Air/Water Interface",

abstract = "A hydrophobic peptide, Boc-(Ala-Aib)8-OMe (BA16M), and its end-modified derivatives were synthesized, and the pressure-area (π-A) isotherms of the peptides spread at the air/water interface were studied from the viewpoint of interhelix interactions. All π-A isotherms of the synthetic peptides showed an inflection and weak irregular bumping at a surface areas of about 240 and 230 {\AA}2/molecule, respectively, indicating that the helix axis of the peptide is oriented parallel to the interface. A small mound was observed at around 300 {\AA}2/molecule in the π-a isotherm of BA16M, which was ascribed to the phase transition from a liquid to a solid state. The monolayer of an equimolar mixture of the peptides having an opposite kind of charge in the end group underwent the phase transition in the π-A isotherm, which was not observed with one of the two peptides. The electrostatic interaction between the end groups should stabilize the molecular packing at the interface.",

author = "Katsuhiko Fujita and Shunsaku Kimura and Yukio Imanishi and Elmar Rump and Helmut Ringsdorf",

year = "1994",

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AU - Fujita, Katsuhiko

AU - Kimura, Shunsaku

AU - Imanishi, Yukio

AU - Rump, Elmar

AU - Ringsdorf, Helmut

PY - 1994/8/1

Y1 - 1994/8/1

N2 - A hydrophobic peptide, Boc-(Ala-Aib)8-OMe (BA16M), and its end-modified derivatives were synthesized, and the pressure-area (π-A) isotherms of the peptides spread at the air/water interface were studied from the viewpoint of interhelix interactions. All π-A isotherms of the synthetic peptides showed an inflection and weak irregular bumping at a surface areas of about 240 and 230 Å2/molecule, respectively, indicating that the helix axis of the peptide is oriented parallel to the interface. A small mound was observed at around 300 Å2/molecule in the π-a isotherm of BA16M, which was ascribed to the phase transition from a liquid to a solid state. The monolayer of an equimolar mixture of the peptides having an opposite kind of charge in the end group underwent the phase transition in the π-A isotherm, which was not observed with one of the two peptides. The electrostatic interaction between the end groups should stabilize the molecular packing at the interface.

AB - A hydrophobic peptide, Boc-(Ala-Aib)8-OMe (BA16M), and its end-modified derivatives were synthesized, and the pressure-area (π-A) isotherms of the peptides spread at the air/water interface were studied from the viewpoint of interhelix interactions. All π-A isotherms of the synthetic peptides showed an inflection and weak irregular bumping at a surface areas of about 240 and 230 Å2/molecule, respectively, indicating that the helix axis of the peptide is oriented parallel to the interface. A small mound was observed at around 300 Å2/molecule in the π-a isotherm of BA16M, which was ascribed to the phase transition from a liquid to a solid state. The monolayer of an equimolar mixture of the peptides having an opposite kind of charge in the end group underwent the phase transition in the π-A isotherm, which was not observed with one of the two peptides. The electrostatic interaction between the end groups should stabilize the molecular packing at the interface.

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Monolayer Properties of Hydrophobic α-Helical Peptides Having Various End Groups at the Air/Water Interface

Abstract

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