Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.biomaterials.2008.03.020
Title: Identification, recombinant production and structural characterization of four silk proteins from the Asiatic honeybee Apis cerana
Authors: Shi, J. 
Song, J. 
Lua, S.
Du, N. 
Liu, X. 
Keywords: Asiatic honeybee Apis cerana
Circular dichroism
Coiled-coil
Dynamic light scattering
Recombinant biotechnology
Silk protein
Issue Date: 2008
Source: Shi, J., Song, J., Lua, S., Du, N., Liu, X. (2008). Identification, recombinant production and structural characterization of four silk proteins from the Asiatic honeybee Apis cerana. Biomaterials 29 (18) : 2820-2828. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biomaterials.2008.03.020
Abstract: Unlike silkworm and spider silks assembled from very large and repetitive fibrous proteins, the bee and ant silks were recently demonstrated to consist of four small and non-repetitive coiled-coil proteins. The design principle for this silk family remains largely unknown and so far no structural study is available on them in solution. The present study aimed to identify, express and characterize the Asiatic honeybee silk proteins using DLS, CD and NMR spectroscopy. Consequently, (1) four silk proteins are identified, with ∼6, 10, 9 and 8% variations, respectively, from their European honeybee homologs. Strikingly, their recombinant forms can be produced in Escherichia coil with yields of 10-60 mg/l. (2) Despite containing ∼65% coiled-coil sequences, four proteins have very low α-helix (9-27%) but unusually high random coil (45-56%) contents. Surprisingly, β-sheet is also detected in four silk proteins (26-35%), implying the possible presence of β-sheet in the bee and ant silks. (3) Four proteins lacking of the tight tertiary packing appear capable of interacting with each other weakly but this interaction triggers no significant formation of the tight tertiary packing. The study not only implies the promising potential to produce recombinant honeybee silk proteins for the development of various biomaterials; but also provides the first structural insight into the molecular mechanism underlying the formation of the coiled-coil silks. © 2008 Elsevier Ltd. All rights reserved.
Source Title: Biomaterials
URI: http://scholarbank.nus.edu.sg/handle/10635/28856
ISSN: 01429612
DOI: 10.1016/j.biomaterials.2008.03.020
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