Sharifahmadian, Mahzad and Booth, Valerie and Waring , Alan J. and Sarker, Muzaddid and Palleboina, Dharamaraju and Morrow, Michael R. and Walther , Frans J. (2013) Role of the N-Terminal Seven Residues of Surfactant Protein B (SP-B). PLoS ONE, 8 (9). ISSN 1932-6203
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Breathing is enabled by lung surfactant, a mixture of proteins and lipids that forms a surface-active layer and reduces surface tension at the air-water interface in lungs. Surfactant protein B (SP-B) is an essential component of lung surfactant. In this study we probe the mechanism underlying the important functional contributions made by the N-terminal 7 residues of SP-B, a region sometimes called the “insertion sequence”. These studies employed a construct of SP-B, SP-B (1–25,63–78), also called Super Mini-B, which is a 41-residue peptide with internal disulfide bonds comprising the N-terminal 7-residue insertion sequence and the N- and C-terminal helices of SP-B. Circular dichroism, solution NMR, and solid state 2H NMR were used to study the structure of SP-B (1–25,63–78) and its interactions with phospholipid bilayers. Comparison of results for SP-B (8–25,63–78) and SP-B (1–25,63–78) demonstrates that the presence of the 7-residue insertion sequence induces substantial disorder near the centre of the lipid bilayer, but without a major disruption of the overall mechanical orientation of the bilayers. This observation suggests the insertion sequence is unlikely to penetrate deeply into the bilayer. The 7-residue insertion sequence substantially increases the solution NMR linewidths, most likely due to an increase in global dynamics.
|Additional Information:||Memorial University Open Access Author's Fund|
|Department(s):||Science, Faculty of > Biochemistry|
|Date:||2 September 2013|
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