The presence of elastic fibres in the extracellular matrix (ECM) provides physiologically important elastic properties for many tissues. Until recently, microfibrils, one component of the ECM, were thought primarily to serve as a scaffolding on which elastin is deposited during development to form elaunin fibres [1]. The most prominent protein that forms mammalian microfibrils is fibrillin. It is known that mutations in the fibrillin gene cause a heterogenous connective tissue disease called Marfan syndrome [2], so information on mechanical properties of microfibrils or their role in tissue function would be useful. Microfibrils are also found in the ECM of some invertebrate tissues, and there is growing evidence that the protein forming the structure is homologous to mammalian fibrillin [3,4]. It has been shown that the microfibril-based arterial wall of the lobster has viscoelastic properties [5], and we have now utilized this primitive artery to measure the modulus of elasticity of microfibrils. It is similar to that of the rubber-like protein elastin.
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