Designer peptide surfactants stabilize functional photosystem-I membrane complex in aqueous solution for extended time .

Detailed structural analyses of membrane proteins as well as their uses in advanced nanobiotechnological applications require extended stabilization of the functional protein conformation. Here we report that a new class of designer surfactant like peptides can significantly increase the activity and stabilize the functional form of the multidomain protein complex Photosystem-I (PS-I) in solution better than other commonly used chemical detergents. We carried out a systematic analysis using a series of such peptides to identify the chemical and structural features that enhance the photochemical activity of PS-I. We observed that peptide surfactant amphiphilicity is necessary but not sufficient to stabilize PS-I in its functional form. A number of factors are essential for designing the optimal peptide including amino acid sequence, N-terminal acetylation and C-terminal amidation. Furthermore, we showed that the polarity and number of charges on the hydrophilic head are important as well as hydrophobicity and size of the amino acid side groups in the hydrophobic tail play an important role. The best performing peptides for the stabilization of functional PS-I are, in order of effectiveness, ac-I(6)K(2)-CONH(2), ac-A(6)K-CONH(2), ac-V(6)K(2)-CONH(2), and ac-V(6)R(2)-CONH(2). These simple and inexpensive peptide surfactants will likely make significant contributions to stabilize the functional form of diverse and currently elusive membrane proteins and their complexes with important applications.