Nova Scotia Research Team Analyzes Structure of Spider Silk’s AcSp1’s Repeat Sequence at Very High Resolution; Repeat Units Behave in Modular Fashion; Findings Advance Development of Artificial Silks

Incredibly tough, slightly stretchy spider silk is a lightweight, biodegradable wonder material with numerous potential biomedical applications. But although humans have been colonizing relatively placid silkworms for thousands of years, harvesting silk from territorial and sometimes cannibalistic spiders has proven impractical. Instead, labs hoping to harness spider silk's mechanical properties are using its molecular structure as a template for their own biomimetic silks. A team of researchers from Dalhousie University in Nova Scotia is focusing on the toughest of the spider's seven types of silk--aciniform silk, used to wrap up prey that blunders into the spider’s web. Over the past few years, the scientists have gradually unraveled its protein architecture and begun to understand the connection between its structure and its function. The researchers presented their latest findings in a poster session during the 59th meeting of the Biophysical Society, held Feb. 7-11 in Baltimore, Maryland. The poster, "Roles of Spider Wrapping Silk Protein Domains in Fibre Properties" by Lingling Xu, Marie-Laurence Tremblay, Kathleen E. Orrell, Xiang-Qin Liu and Jan K. Rainey, was displayed on Tuesday, February 10, 2015. The first step in creating artificial spider silk is to replicate the proteins that make up the natural version, in this case, by recombinantly expressing them in E. coli. The key protein in aciniform silk, AcSp1, has three parts. Most of the protein is a repeated sequence of about two hundred amino acids. Two tails called the N- and C-terminal domains hang off each end of the protein chain.
Login Or Register To Read Full Story