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首页> 外文期刊>Biochemistry >Modifications to Surfactant Protein B Structure and Lipid Interactions under Respiratory Distress Conditions: Consequences of Tryptophan Oxidation
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Modifications to Surfactant Protein B Structure and Lipid Interactions under Respiratory Distress Conditions: Consequences of Tryptophan Oxidation

机译：呼吸窘迫条件下对表面活性蛋白B结构和脂质相互作用的修饰：色氨酸氧化的后果。

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These studies detail the altered structure-function relationships caused by oxidation of surfactant protein B (SP-B), a mode of damage thought to be important in acute respiratory distress syndrome (ARDS), a common and frequently fatal condition. An 18-residue fragment comprising the N-terminal helix of SP-B was investigated in oxidized and unmodified forms by solution and solid-state nuclear magnetic resonance (NMR), circular dichroism (CD), and molecular dynamics (MD) simulation. Taken together, the results indicate that tryptophan oxidation causes substantial disruptions in helical structure and lipid interactions. The structural modifications induced by tryptophan oxidation were severe, with a reduction in helical extent from approximately three helical turns to, at most, one turn, and were observed in a variety of solvent environments, including sodium dodecyl sulfate (SDS) micelles, dodecyl phosphocholine (DPC) micelles, and a 40% hexafluoro-2-propanol (HFIP) aqueous solution. The unmodified peptide takes on an orientation within lipid bilayers that is tilted approximately 30 degrees away from an in-plane position. Tryptophan oxidation causes significant modifications to the peptide-lipid interactions, and the peptide likely shifts to a more in-plane orientation within the lipids. Interestingly, the character of the disruptions to peptide-lipid interactions caused by tryptophan oxidation was highly dependent on the charge of the lipid headgroup.
机译：这些研究详细描述了表面活性剂蛋白B（SP-B）的氧化引起的结构-功能关系的改变，表面活性剂蛋白B（SP-B）的一种损伤方式在急性呼吸窘迫综合征（ARDS）中是很常见的，这是一种常见的致命疾病。通过溶液和固态核磁共振（NMR），圆二色性（CD）和分子动力学（MD）模拟，研究了氧化和未修饰形式的包含SP-B N末端螺旋的18个残基片段。两者合计，结果表明色氨酸氧化导致螺旋结构和脂质相互作用的实质性破坏。色氨酸氧化引起的结构修饰很严重，螺旋范围从大约三个螺旋圈减少到最多一个螺旋圈，并且在包括十二烷基硫酸钠（SDS）胶束，十二烷基磷酸胆碱在内的各种溶剂环境中观察到（DPC）胶束和40％六氟-2-丙醇（HFIP）水溶液。未修饰的肽在脂质双层中具有从平面内位置倾斜大约30度的方向。色氨酸氧化引起肽-脂相互作用的显着修饰，并且肽可能在脂质内转移到更平面内的方向。有趣的是，由色氨酸氧化引起的肽-脂质相互作用破坏的特征高度依赖于脂质头基的电荷。

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