Self-assembly of avidin and D-biotin-tethering zeolite microcrystals into fibrous aggregates

被引:23
作者
Um, SH
Lee, GS
Lee, YJ
Koo, KK
Lee, C
Yoon, KB [1 ]
机构
[1] Sogang Univ, Dept Chem, Seoul 121742, South Korea
[2] Sogang Univ, Dept Chem Engn, Seoul 121742, South Korea
[3] Sogang Univ, Ctr Microcrystal Assembly, Seoul 121742, South Korea
[4] Ewha Womans Univ, Dept Chem, Seoul 120750, South Korea
关键词
D O I
10.1021/la020118o
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Avidin and nanometer-sized zeolite crystals (similar to300 nm) tethered with D-biotin readily self-assemble into thin (2-20 mum) and very long (> 1 cm) fibrous aggregates in a buffer solution of pH = 7.4 when the avidin-to-zeolite weight ratio (A/Z) is equal to or higher than 0.2. At A/Z = 0.2, the exteriors of the produced fibrils are covered with zeolite-A crystals. At A/Z = 0.4, the zeolite crystals are completely buried within the fibrils covered with thick layers of avidin. At A/Z = 0.8-1.0, the morphology of the fibrils becomes smooth and flat due to the thick surface-lining avidin layers. The zeolite and avidin remain intact within the fibrils. Control experiments reveal that complexation between avidin and the zeolite-bound biotin is essential for fibrillation to occur. Interestingly, discrete clusters of zeolite crystals with sizes of 5-10 mum are produced when the A/Z ratio is reduced to 0.1. The observed fibrillation is very much like the previously reported case with beta-glucosidase and D-glucose-tethering zeolite microcrystals, despite that the type of the protein-substrate pair is different. This result therefore raises the possibility that self-assembly of complex forming proteins and the nanoparticles or microparticles tethered with the corresponding substrates into fibrils is a general phenomenon.
引用
收藏
页码:4455 / 4459
页数:5
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