Influence of subphase on the orientation of helical peptides at interface
| Autor: | Junzo Umemura, Tomoyuki Morita, Shunsaku Kimura, Kazuya Kitagawa |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
Polymers and Plastics Chemistry Stereochemistry molecular assembly Organic Chemistry helical peptide Peptide Oligomer Crystallography Dipole chemistry.chemical_compound Orientation (geometry) Monolayer Materials Chemistry interface Methanol Spectroscopy Electrostatic interaction |
| Zdroj: | Polymer. 43:3533-3540 |
| ISSN: | 0032-3861 |
| DOI: | 10.1016/s0032-3861(02)00044-7 |
| Popis: | Boc-( l -Leu-Aib) n -OBzl ( n =8, 12, 16; OBzl represents benzyl ester) was spread on water or a mixture of water and methanol (1/1 v/v) and the orientation of the helical peptides on subphase was investigated by FTIR-reflection–absorption spectroscopy. When the peptides were spread at a liquid phase on subphase, the peptides took a vertical orientation, which was not attainable by compression of peptide monolayers initially spread at a gas phase on subphase. However, the peptide monolayers on water could not be transferred on gold with keeping the vertical orientation. On the other hand, when the peptides were spread on a mixture of water and methanol, the orientation of helical peptides was closer to vertical than that on water and the monolayers were transferred repeatedly on gold to form multilayers with a vertical orientation. The suppression of orientation change upon transfer of the peptide monolayer is considered to be due to reduction of electrostatic interaction between the peptide and the image dipole when the peptide is spread on a mixture of water and methanol. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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