Abstract
Spider silk attracts researchers from the most diverse fields, such as material science or medicine. However, still little is known about silk aside from its molecular structure and material strength. Spiders produce many different silks and even join several silk types to one functional unit. In cribellate spiders, a complex multi-fibre system with up to six different silks affects the adherence to the prey. The assembly of these cribellate capture threads influences the mechanical properties as each fibre type absorbs forces specifically. For the interplay of fibres, spinnerets have to move spatially and come into contact with each other at specific points in time. However, spinneret kinematics are not well described though highly sophisticated movements are performed which are in no way inferior to the movements of other flexible appendages. We describe here the kinematics for the spinnerets involved in the cribellate spinning process of the grey house spider, Badumna longinqua, as an example of spinneret kinematics in general. With this information, we set a basis for understanding spinneret kinematics in other spinning processes of spiders and additionally provide inspiration for biomimetic multiple fibre spinning.
Highlights
Spider silk captivates researchers for many decades not least because of its extraordinary material properties (Vollrath 2000; Eisoldt et al 2011)
We aim to analyse the spinneret kinematics using the cribellate spinning process, in which almost all spinnerets are involved in the process and a highly repetitive threedimensional structure is created as a thread
We investigated the spinneret kinematics of the synanthropic cribellate grey house spider Badumna longinqua (Desidae)
Summary
Spider silk captivates researchers for many decades not least because of its extraordinary material properties (Vollrath 2000; Eisoldt et al 2011). One of the most studied characteristics to uncover the principle behind the high toughness of spider silk is its molecular structure, which enhances toughness by a combination of elastic and crystalline domains in the protein (Termonia 1994; Hayashi et al 1999; Becker et al 2003; Mortimer and Holland 2015). There is not a single type of spider silk: Spiders
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