Identification of hornet silk gene with a characteristic repetitive sequence in Vespa simillima xanthoptera

Kameda, Tsunenori; Kojima, Katsura; Zhang, Qiang; Sezutsu, Hideki

doi:10.1016/j.cbpb.2011.09.002

Cited by 6 publications

(3 citation statements)

References 25 publications

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“…The SDS‐PAGE pattern for hornet silk dialyzed in DW (DW in Figure ) exhibited four bands similar to those for cocoons. Although multiple thin bands due to cross‐links and/or degradation also appeared alongside the four major bands after dialysis, sharp bands with no smearing appeared for all dialysis temperatures.…”

Section: Resultsmentioning

confidence: 99%

Influence of pH, temperature, and concentration on stabilization of aqueous hornet silk solution and fabrication of salt‐free materials

Kameda

2014

Biopolymers

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We found that an aqueous solution of silk from cocoons produced by hornet larvae (hornet silk) can be obtained when the solution is adjusted to basic conditions of pH > 9.2. It is known that native hornet cocoons can be dissolved in concentrated aqueous solution of salts, such as lithium bromide (LiBr) and calcium chloride (CaCl2). Upon the removal of these salts from solution by dialysis, solidification, gelation, or sedimentation of hornet silk is known to occur. In the present study, under basic conditions, however, no such solidification occurred, even after salt removal. In this study, ammonia was used for alkalization of solution because it is volatilized during the casting process and pure hornet silk materials can be obtained after drying. The effects of the concentrations of hornet silk and ammonia, as well as dialysis temperature, on preventing gelation during dialysis were investigated. Dialysis conditions that limit the degradation of hornet silk by hydrolysis in alkali solution were identified. Moreover, casting conditions to prepare flexible and transparent hornet silk film from aqueous ammonia solution were optimized. Molecular structural analysis of hornet silk in aqueous ammonia solution and cast film indicated the formation of α-helix conformations.

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Section: Resultsmentioning

confidence: 99%

Influence of pH, temperature, and concentration on stabilization of aqueous hornet silk solution and fabrication of salt‐free materials

Kameda

2014

Biopolymers

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“…[2][3][4] The structure of hornet silk has been reported in our recent studies. [5][6][7][8][9][10][11][12] The amino-acid sequences of six types of hornet silk proteins of Vespa simillima xanthoptera Cameron have been determined. 5,6,10 Of these six proteins, four are major and have similar characteristics.…”

Section: Introductionmentioning

confidence: 99%

“…[5][6][7][8][9][10][11][12] The amino-acid sequences of six types of hornet silk proteins of Vespa simillima xanthoptera Cameron have been determined. 5,6,10 Of these six proteins, four are major and have similar characteristics. These four major proteins consist of an alanine(Ala)-rich domain at the center of the chain and serine(Ser)-rich domains at both ends of the chain.…”

Section: Introductionmentioning

confidence: 99%

Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

Kameda

2012

Polym J

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Here, we demonstrate the first successful isotope labeling of Ala carbons in hornet silk produced by the larvae of Vespa (Vespinae, Vespidae) mandarinia. This labeled hornet silk was examined by high-resolution 13 C solid-state NMR, and it was found that the fraction of Ala residues in a-helical conformations compared with Ala residues in the overall conformation of hornet silk can be quantitatively determined from Ala C a NMR peaks. The value for this a-helical Ala fraction is close to that of the fraction of Ala residues in coiled-coil structures estimated in the four major hornet silk proteins by coiled-coil prediction analysis. This result indicates that most of the Ala residues in a-helices occur in those a-helices with a coiled-coil structure, and that the number of Ala residues in a-helices without a coiled-coil structure is small. Moreover, coiled-coil prediction analysis indicated that the potential coiled-coil domains are located only in the central portion of the protein chains of the major hornet silk proteins. From these results, we confirmed that the a-helical conformation mostly forms in the central portion of the hornet silk chains, whereas the ends of the protein chains are nearly devoid of a-helical structure. We deduce that the ends of the protein chains would preferentially adopt a b-sheet conformation.

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Evolution and Application of Coiled Coil Silks from Insects

Kameda¹,

Walker²,

Sutherland³

2013

Biotechnology of Silk

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Identification of hornet silk gene with a characteristic repetitive sequence in Vespa simillima xanthoptera

Cited by 6 publications

References 25 publications

Influence of pH, temperature, and concentration on stabilization of aqueous hornet silk solution and fabrication of salt‐free materials

Influence of pH, temperature, and concentration on stabilization of aqueous hornet silk solution and fabrication of salt‐free materials

Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

Evolution and Application of Coiled Coil Silks from Insects

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