化學法轉化奈米矽片應用於光學膜硬度與蛋白質結合

Abstract

本研究旨在討論奈米矽片的改質與應用。由於矽片的邊緣有許多官能基，其每片約有18,000個 ≡Si–O-Na+ 以及100,000-300,000個 ≡Si–OH 官能基作為反應點，因此可藉由化學反應將小分子以共價鍵的方式連接至矽片邊緣。在此，利用琥珀酸二甲酯與矽片邊緣的官能基(≡Si–O-Na+)進行酯交換反應得NSP–DMS；以及利用四乙氧基矽烷與矽片邊緣的官能基(≡Si–OH)進行溶膠凝膠反應得NSP–TEOS。並且，利用熱重力分析、固態矽譜、穿透式顯微鏡等儀器鑑定NSP–DMS以及NSP–TEOS。而更進一步的，我們將NSP–DMS和NSP–TEOS分別摻入壓克力樹脂並將其於玻璃基材上成膜，可使其膜硬度有效提高並具有高度透明性。 另一部份，根據前面將小分子修飾於矽片邊緣的研究基礎，更進一步的嘗試利用共價連接大分子於矽片邊緣，如溶菌酶，生成NSP–lysozyme並以熱重力分析之。而於檢測NSP–lysozyme活性時，卻意外的發現矽片接枝lysozyme或矽片混摻lysozyme皆可以使lysozyme殺菌能力降低，進而可得知矽片亦可使蛋白質降低活性。

The object of this research is to study the modification and applications of Nanoscale Silicate Platelets (NSP) that were previously prepared from the exfoliation of naturally occurring clays. The silicate platelets were allowed to tether linkers through covalent bonding with the estimated number of 18,000 ≡Si–O-Na+ sites and 100,000-300,000 siloxanol functionalities (≡Si–OH) per platelet. The silicate platelets were then modified by grafting the linker, dimethyl succinate, via transesterification to afford NSP–DMS. The second method is to use sol–gel reaction with tetraethyl orthosilicate as the linker to form NSP–TEOS. Both of NSP–DMS and NSP–TEOS were characterized by using thermogravimetric analysis, silicon nuclear magnetic resonance, and transmission electron microscopy. The two NSP–linkers were used to blend into a typical formulation of acrylic resins. The effectiveness for enhancing hardness of the resultant films while maintaining the excellent transparency was achieved. According to the previous works of small molecule tethering, we further established the NSP tethering with a macromolecule, such as lysozyme, through an amide functionality. The NSP–lysozyme conjugate was also characterized by using thermogravimetric analysis. During the testing for the lysozyme activity, a serendipity was found for the NSP strongly interacting with an enzyme and actually deactivating the biomaterial’s normal function of antimicrobial ability. The finding was observed in both of NSP physical blending and covalently bonding with the lysozyme enzyme. The finding has the implications of designing new method of protein fixation.