The molecular basis of nonlinear optical (NLO) chiral effects in the amide I region of type I collagen was investigated using sum-frequency generation vibrational spectroscopy; chiral and achiral tensor elements were separated using different input/output beam polarization conditions. Spectra were obtained from native rat tail tendon (RTT) collagen and from cholesteric liquid crystal-like (LC) type I collagen films. Although RTT and LC collagen both possess long-range order, LC collagen lacks the complex hierarchical organization of RTT collagen. Their spectra were compared to assess the role of such organization in NLO chirality. No significant differences were observed between RTT and LC with respect to chiral or achiral spectra. These findings suggest that amide I NLO chiral effects in type I collagen assemblies arise predominantly from the chiral organization of amide chromophores within individual collagen molecules, rather than from supramolecular structures. The study suggests that sum-frequency generation vibrational spectroscopy may be uniquely valuable in exploring fundamental aspects of chiral nonlinearity in complex macromolecular structures.

译文

使用和频产生振动光谱研究了I型胶原的酰胺I区域中非线性光学 (NLO) 手性效应的分子基础; 使用不同的输入/输出光束偏振条件分离手性和非手性张量元素。光谱是从天然的大鼠尾腱 (RTT) 胶原蛋白和胆甾型液晶样 (LC) I型胶原蛋白膜获得的。尽管RTT和LC胶原蛋白都具有长程顺序,但LC胶原蛋白缺乏RTT胶原蛋白的复杂层次组织。比较了它们的光谱,以评估这种组织在NLO手性中的作用。在手性或无手性光谱方面,RTT和LC之间未观察到显着差异。这些发现表明,I型胶原蛋白组装体中的酰胺I NLO手性作用主要来自单个胶原蛋白分子中酰胺发色团的手性组织,而不是超分子结构。研究表明,和频产生振动光谱在探索复杂大分子结构中手性非线性的基本方面可能具有独特的价值。

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