Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time.
We used a class of designed peptide detergents to stabilize photosystem I (PS-I) upon extended drying under N2 on a gold-coated-Ni-NTA glass surface. PS-I is a chlorophyll-containing membrane protein complex that is the primary reducer of ferredoxin and the electron acceptor of plastocyanin. We isol...
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2005-07-01
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Online Access: | http://dx.doi.org/10.1371/journal.pbio.0030230 |
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doaj-043e44f61f9c4f2abc10b531fde97fe72021-07-02T09:47:09ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852005-07-0137e230Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time.We used a class of designed peptide detergents to stabilize photosystem I (PS-I) upon extended drying under N2 on a gold-coated-Ni-NTA glass surface. PS-I is a chlorophyll-containing membrane protein complex that is the primary reducer of ferredoxin and the electron acceptor of plastocyanin. We isolated the complex from the thylakoids of spinach chloroplasts using a chemical detergent. The chlorophyll molecules associated with the PS-I complex provide an intrinsic steady-state emission spectrum between 650 and 800 nm at -196.15 degrees C that reflects the organization of the pigment-protein interactions. In the absence of detergents, a large blue shift of the fluorescence maxima from approximately 735 nm to approximately 685 nm indicates a disruption in light-harvesting subunit organization, thus revealing chlorophyll-protein interactions. The commonly used membrane protein-stabilizing detergents, N-dodecyl-beta-D-maltoside and N-octyl-beta-D-glucoside, only partially stabilized the approximately 735-nm complex with approximately 685-nm spectroscopic shift. However, prior to drying, addition of the peptide detergent acetyl-AAAAAAK at increasing concentration significantly stabilized the PS-I complex. Moreover, in the presence of acetyl-AAAAAAK, the PS-I complex is stable in a dried form at room temperature for at least 3 wk. Another peptide detergent, acetyl-VVVVVVD, also stabilized the complex but to a lesser extent. These observations suggest that the peptide detergents may effectively stabilize membrane proteins in the solid-state. These designed peptide detergents may facilitate the study of diverse types of membrane proteins.http://dx.doi.org/10.1371/journal.pbio.0030230 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
title |
Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. |
spellingShingle |
Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. PLoS Biology |
title_short |
Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. |
title_full |
Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. |
title_fullStr |
Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. |
title_full_unstemmed |
Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. |
title_sort |
self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Biology |
issn |
1544-9173 1545-7885 |
publishDate |
2005-07-01 |
description |
We used a class of designed peptide detergents to stabilize photosystem I (PS-I) upon extended drying under N2 on a gold-coated-Ni-NTA glass surface. PS-I is a chlorophyll-containing membrane protein complex that is the primary reducer of ferredoxin and the electron acceptor of plastocyanin. We isolated the complex from the thylakoids of spinach chloroplasts using a chemical detergent. The chlorophyll molecules associated with the PS-I complex provide an intrinsic steady-state emission spectrum between 650 and 800 nm at -196.15 degrees C that reflects the organization of the pigment-protein interactions. In the absence of detergents, a large blue shift of the fluorescence maxima from approximately 735 nm to approximately 685 nm indicates a disruption in light-harvesting subunit organization, thus revealing chlorophyll-protein interactions. The commonly used membrane protein-stabilizing detergents, N-dodecyl-beta-D-maltoside and N-octyl-beta-D-glucoside, only partially stabilized the approximately 735-nm complex with approximately 685-nm spectroscopic shift. However, prior to drying, addition of the peptide detergent acetyl-AAAAAAK at increasing concentration significantly stabilized the PS-I complex. Moreover, in the presence of acetyl-AAAAAAK, the PS-I complex is stable in a dried form at room temperature for at least 3 wk. Another peptide detergent, acetyl-VVVVVVD, also stabilized the complex but to a lesser extent. These observations suggest that the peptide detergents may effectively stabilize membrane proteins in the solid-state. These designed peptide detergents may facilitate the study of diverse types of membrane proteins. |
url |
http://dx.doi.org/10.1371/journal.pbio.0030230 |
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1721332724579434496 |