The Department of Molecular, Cellular and Developmental Biology
About the Department Academic Programs Research Seminars & Events Directory Spacer Search MCDB MCDB Home

MCDB Home > Faculty > Herbert Waite > Current Research

Current Research


Figure 1

It is self-evident that man-made adhesives do not stick very well to wet surfaces. This simple technological limitation has had a profound influence on the way that manufacturing, medical, and building practices have evolved in human society. Marine organisms such as barnacles, limpets, kelps, and mussels, however, produce glues that do very well underwater. Until recently, little was known about the chemical and physical mechanisms of such biological attachment, except that some organisms rely on temporary adhesives, while in others, adhesion is permanent.

Mussels such as Mytilus attach themselves to surfaces by making a bundle of threads collectively referred to as the byssus. Byssal threads are permanent holdfasts and extraordinary biomolecular materials; they are strong, rapidly made, durable and adhere to a wide variety of surfaces including glass, metal, paraffin and bone. A careful morphological examination of byssus reveals it to be a complex composite material with at least four functional domains: load-bearing fibers, microcellular solids, sealants and adhesion promoters. Our research is committed to understanding how byssal threads are made and, in particular, how they adhere to wet surfaces. The first step is the characterization of proteins from each functional domain. This was very difficult given the leathery and insoluble nature of the byssus.

A few years ago, we accidentally discovered that byssal curing could be impeded by subjecting mussels to a cold temperature shock. This seemingly simple perturbation has lead to characterization of a font of exotic proteins previously locked in place by a cross-linked network. We are using protein chemistry, molecular biology and a variety of physical methods including laser mass spectrometry, solid-state nmr and atomic force microscopy to reveal sequence, structure and solution behavior. Our aim is ultimately to process the appropriate protein(s) into useful applications that mimic their adapted functions in the mussels.

Button Bar

Faculty Home Current Research Selected Publications


Department | Academic Programs | Research | Seminars & Events | Directory | Search | Home

UCSB Logo