Abstract
Honeybee larvae produce a silk made up of proteins in predominantly a coiled coil molecular structure. These proteins can be produced in recombinant systems, making them desirable templates for the design of advanced materials. However, the atomic level structure of these proteins is proving difficult to determine: firstly, because coiled coils are difficult to crystalize; and secondly, fibrous proteins crystalize as fibres rather than as discrete protein units. In this study, we synthesised peptides from the central structural domain, as well as the N- and C-terminal domains, of the honeybee silk. We used circular dichroism spectroscopy, infrared spectroscopy, and molecular dynamics to investigate the folding behaviour of the central domain peptides. We found that they folded as predicted by bioinformatics analysis, giving the protein engineer confidence in bioinformatics predictions to guide the design of new functionality into these protein templates. These results, along with the infrared structural analysis of the N- and C-terminal domain peptides and the comparison of peptide film properties with those of the full-length AmelF3 protein, provided significant insight into the structural elements required for honeybee silk protein to form into stable materials.
Highlights
Honeybee larvae spin silken cocoons in which they pupate
Fourier Transform Infrared (FTIR) spectroscopy was utilized to determine the secondary structure of peptides derived from different regions of the honeybee silk protein AmelF3 (Figure 1), in the solid-state
We propose that the length of the coiled coil domain has evolved as to be optimal, in relation to the width of the coiled coil unit, for native materials fabrication
Summary
Honeybee larvae spin silken cocoons in which they pupate. These cocoons accumulate in the honeybee hive and form the basis of the brood comb for successive generations of larvae.The accumulating silk contributes to the thermal and mechanical stability of the hive [1].Honeybee silk has a distinctive molecular structure that is unlike the primarily β-sheet structure of spider and silkworm silks. Honeybee larvae spin silken cocoons in which they pupate. These cocoons accumulate in the honeybee hive and form the basis of the brood comb for successive generations of larvae. The accumulating silk contributes to the thermal and mechanical stability of the hive [1]. Honeybee silk has a distinctive molecular structure that is unlike the primarily β-sheet structure of spider and silkworm silks. Fibres drawn from honeybee silk glands are predominantly coiled coil with much lower levels of β-sheet conformation (summarised in Sutherland et al [2]). Native honeybee silk remaining in the presence of wax has a molecular structure consisting of isolated α-helices rather than coiled coils [3]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
