Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time.

Self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time.

Blog Article

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 Muslin Cloth 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 Hospital Bed Accessories solid-state.These designed peptide detergents may facilitate the study of diverse types of membrane proteins.