کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1959731 1057945 2005 15 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Molecular Dynamics Simulations of the Anchoring and Tilting of the Lung-Surfactant Peptide SP-B1-25 in Palmitic Acid Monolayers
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Molecular Dynamics Simulations of the Anchoring and Tilting of the Lung-Surfactant Peptide SP-B1-25 in Palmitic Acid Monolayers
چکیده انگلیسی

We have performed molecular dynamics simulations of multiple copies of the lung-surfactant peptide SP-B1-25 in a palmitic acid (PA) monolayer. SP-B1-25 is a shorter version of lung-surfactant protein B, an important component of lung surfactant. Up to 30 ns simulations of 20 wt % SP-B1-25 in the PA monolayers were performed with different surface areas of PA, extents of PA ionization, and various initial configurations of the peptides. Starting with initial peptide orientation perpendicular to the monolayer, the predicted final tilt angles average 54°∼ 62° with respect to the monolayer normal, similar to those measured experimentally by Lee et al. (Biophysical Journal. 2001. Synchrotron x-ray study of lung surfactant-specific protein SP-B in lipid monolayers. 81:572–585). In their final conformations, hydrogen-bond analysis and amino acid mutation studies show that the peptides are anchored by hydrogen bond interactions between the cationic residues Arg-12 and Arg-17 and the hydrogen bond acceptors of the ionized PA headgroup, and the tilt angle is affected by the interactions of Tyr-7 and Gln-19 with the PA headgroup. Our work indicates that the factors controlling orientation of small peptides in lipid layers can now be uncovered through molecular dynamics simulations.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 89, Issue 6, December 2005, Pages 3807–3821
نویسندگان
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