Relating molecular behaviour to fibre properties of understudied spider silks
Jan K. Rainey
Professor
Department of Biochemistry & Molecular Biology, Department of Chemistry, and School of Biomedical Engineering
Dalhousie University
August 11, 2026
3 p.m.
In-person and online: C2-361
Abstract: Spider silks are renowned for being strong and extensible, with comparisons often made to bulk materials such as Kevlar, steel, or rubber. Much of our knowledge on spider silks, however, comes from studies of one silk type – major ampullate (or dragline) silk. Despite this focus on dragline silk, typical female orb weaving spiders make seven types of silk, each composed of different proteins and having materials properties that are tailored to specific tasks. Adding to silk diversity, some orb-weavers use sticky capture threads (ecribellate spiders) with others using woolly dry-adhesive capture threads (cribellate spiders). At the other extreme, the Mesothelae suborder consists of spiders that produce only one silk type used for multiple purposes. We apply recombinant protein technology to engineer and produce constructs based on a variety of spider silks. Each silk type tends to be somewhat distinctive in its behaviour, meaning that assembling of these proteins into fibres and other material formats often requires substantial development. Here, I will focus on our efforts to understand structure and dynamics of two less-studied spider silks – the silk used to wrap prey and the silk used as part of an adhesive composite material to attach web silks to other materials. We are working to understand these protein types in their soluble pre-assembly states, where high protein concentrations are maintained without premature assembly, through to their strong and tough fibrous states. Key to this is developing understanding of the molecular transformations that both underlie and enable fibre formation.
Jan K. Rainey is Professor and Undergraduate Coordinator in the Department of Biochemistry & Molecular Biology at Dalhousie University, where he also holds cross-appointments in Chemistry and in Biomedical Engineering. Prior to joining Dalhousie in 2006, he completed his BSc in Biochemistry (co-op) at the University of Guelph, followed by MSc and PhD degrees in Experimental Physical Chemistry with Cynthia Goh at the University of Toronto, and a Postdoctoral Fellowship focused on peptide, protein, and membrane NMR spectroscopy with Brian Sykes at the University of Alberta. At Dalhousie, Dr. Rainey’s research program has focused on understanding protein self-assembly to develop functional biomaterials alongside studying membrane-interactive peptides and peptide-activated integral membrane receptors. Dr. Rainey also frequently works with industrial partners, including a particularly fruitful ongoing collaboration with Halifax-based 3DBioFibR Inc. NMR spectroscopy has been a mainstay in Dr. Rainey’s research program but the inherently “messy” nature of the systems his group studies and the diversity of backgrounds, interests, and goals of his students and postdoctoral fellows mean that a wide variety of methodologies are developed and employed.