In contrast to the primarily β-sheet structuring of spider and silkworm silks, fibers drawn from honeybee silk glands adopt a distinctive and predominantly coiled coil structure. A recombinant version of the honeybee silk protein Apis mellifera Fibrion 3 (AmelF3) can be fabricated into a variety of material forms making it of interest for the design of functionally active protein-based materials. Previous experimental studies have shown that the central domain of AmelF3 supports a tetrameric coiled coil structure while recently published computational work revealed that central domain peptide fragments align in an anti-parallel orientation. However, the AmelF3 terminal domains, responsible for the formation and stabilization of larger silk aggregates, have yet to be studied in detail. Atomic level insight about the folding and alignment of these domains is crucial to understanding why honeybee silk protein structuring is so unique and the strengths it offers. To this end molecular dynamic simulations and bioinformatic protein structure prediction tools were utilized to study folding in C- and N- terminal domain peptides of AmelF3. The predictions of the bioinformatic tools were found to agree well with MD simulations, together providing new insight into the secondary structure distribution and tertiary structure of the 3D folded states of the terminal domains. Differences between solution and solid-state results highlight that significant secondary structural changes in these domains may take place during the silk aggregation process.

Computational study of honeybee silk protein terminal domain secondary structure and dynamics

ACS Spring Meeting 2021

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.