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Sequence Identification, Recombinant Production, and Analysis of the Self-Assembly of Egg Stalk Silk Proteins from Lacewing Chrysoperla carnea

Titelangaben

Neuenfeldt, Martin ; Scheibel, Thomas:
Sequence Identification, Recombinant Production, and Analysis of the Self-Assembly of Egg Stalk Silk Proteins from Lacewing Chrysoperla carnea.
In: Biomolecules. Bd. 43 (13 Juni 2017) Heft 7 .
ISSN 2218-273X
DOI: 10.3390/biom7020043

Abstract

Egg stalk silks of the common green lacewing Chrysoperla carnea likely comprise at least three different silk proteins. Based on the natural spinning process, it was hypothesized that these proteins self-assemble without shear stress, as adult lacewings do not use a spinneret. To examine this, the first sequence identification and determination of the gene expression profile of several silk proteins and various transcript variants thereof was conducted, and then the three major proteins were recombinantly produced in Escherichia coli encoded by their native complementary DNA (cDNA) sequences. Circular dichroism measurements indicated that the silk proteins in aqueous solutions had a mainly intrinsically disordered structure. The largest silk protein, which we named ChryC1, exhibited a lower critical solution temperature (LCST) behavior and self-assembled into fibers or film morphologies, depending on the conditions used. The second silk protein, ChryC2, self-assembled into nanofibrils and subsequently formed hydrogels. Circular dichroism and Fourier transform infrared spectroscopy confirmed conformational changes of both proteins into beta sheet rich structures upon assembly. ChryC3 did not self-assemble into any morphology under the tested conditions. Thereby, through this work, it could be shown that recombinant lacewing silk proteins can be produced and further used for studying the fiber formation of lacewing egg stalks.

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Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: circular dichroism; genome analysis; insect silk; qPCR; recombinant proteins; self-assembly; transcript variants
Institutionen der Universität: Fakultäten
Fakultäten > Fakultät für Ingenieurwissenschaften
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel
Profilfelder
Profilfelder > Advanced Fields
Profilfelder > Advanced Fields > Polymer- und Kolloidforschung
Profilfelder > Advanced Fields > Neue Materialien
Profilfelder > Advanced Fields > Molekulare Biowissenschaften
Profilfelder > Emerging Fields
Profilfelder > Emerging Fields > Lebensmittel- und Gesundheitswissenschaften
Forschungseinrichtungen
Forschungseinrichtungen > Forschungszentren
Forschungseinrichtungen > Forschungszentren > Bayreuther Materialzentrum - BayMAT
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 21 Jun 2017 05:40
Letzte Änderung: 21 Jun 2017 05:40
URI: https://eref.uni-bayreuth.de/id/eprint/38121