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

Title
Self-assembly of avidin and D-biotin-tethering zeolite microcrystals into fibrous aggregates
Authors
Um S.H.Lee G.S.Lee Y.-J.Koo K.-K.Lee C.Yoon K.B.
Ewha Authors
이종목
SCOPUS Author ID
이종목scopus
Issue Date
2002
Journal Title
Langmuir
ISSN
0743-7463JCR Link
Citation
vol. 18, no. 11, pp. 4455 - 4459
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Avidin and nanometer-sized zeolite crystals (∼300 nm) tethered with D-biotin readily self-assemble into thin (2-20 μm) 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 μm are produced when the A/Z ratio is reduced to 0.1. The observed fibrillation is very much like the previously reported case with β-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 complexforming proteins and the nanoparticles or microparticles tethered with the corresponding substrates into fibrils is a general phenomenon.
DOI
10.1021/la020118o
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자연과학대학 > 화학·나노과학전공 > Journal papers
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