Protective materials and structures found in natural organisms may inspire new armors with improved resistance to penetration, flexibility, light weight, and other interesting properties such as transparency and breathability. All these attributes can be found in teleost fish scales, which are the most common types of scales in modern fish species. In this work, we have studied the structure and mechanics of fish scales from striped bass (Morone saxatilis). This scale is about 200–300 µm thick and consists of a hard outer bony layer supported by a softer cross‐ply of collagen fibrils. Perforation tests with a sharp needle indicated that a single fish scale provides a high resistance to penetration which is superior to polystyrene and polycarbonate, two engineering polymers that are typically used for light transparent packaging or protective equipment. Under puncture, the scale undergoes a sequence of two distinct failure events: First, the outer bony layer cracks following a well defined cross‐like pattern which generates four “flaps” of bony material. The deflection of the flaps by the needle is resisted by the collagen layer, which in biaxial tension acts as a retaining membrane. Remarkably this second stage of the penetration process is highly stable, so that an additional 50% penetration force is required to eventually puncture the collagen layer. The combination of a hard layer that can fail in a controlled fashion with a soft and extensible backing layer is the key to the resistance to penetration of individual scales.

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Hard a-keratins such as hair, nail, wool and horn are stiff epidermal appendages used by mammals in a variety of functions including thermoregulation, feeding and intraspecific competition. Hard a-keratins are fibre-reinforced structures consisting of cytoskeletal elements known as 'intermediate filaments' embedded in an amorphous protein matrix. Recent research has shown that intermediate filaments are soft and extensible in living keratinocytes but become far stiffer and less extensible in keratinized cells, and this stiffening may be mediated by air-drying. Baleen, the keratinous plates used by baleen whales during filter feeding, is an unusual mammalian keratin in that it never air dries, and in some species, it represents the most heavily calcified of all the hard a-keratins. We therefore tested the hypothesis that whale baleen is stiffened by calcification. Here, we provide, to our knowledge, the first comprehensive description of baleen material properties and show that calcification contributes to overcoming the shortcomings of stiffening this hard a-keratin without the benefit of air-drying. We also demonstrate striking interspecies differences in the calcification patterns among three species of baleen whales and provide novel insights into the function and evolution of this unusual biomaterial.

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