Elastic modulus and toughness of orb spider glycoprotein glue

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dc.contributor.authorOpell, Brent D.en
dc.contributor.authorClouse, Mary E.en
dc.contributor.authorAndrews, Sheree F.en
dc.contributor.departmentBiological Sciencesen
dc.date.accessioned2019-06-04T16:57:38Zen
dc.date.available2019-06-04T16:57:38Zen
dc.date.issued2018-05-30en
dc.description.abstractAn orb web's prey capture thread features tiny glue droplets, each formed of an adhesive glycoprotein core surrounded by an aqueous layer. Small molecules in the aqueous layer confer droplet hygroscopicity and maintain glycoprotein viscoelasticity, causing droplet volume and glycoprotein performance to track changes in environmental humidity. Droplet extension combines with that of a thread's supporting flagelliform fibers to sum the adhesive forces of multiple droplets, creating an effective adhesive system. We combined measurements of the force on an extending droplet, as gauged by the deflection of its support line, with measurements of glycoprotein volume and droplet extension to determine the Young's modulus (E) and toughness of three species' glycoproteins. We did this at five relative humidities between 20 - 90% to assess the effect of humidity on these properties. When droplets of a thread span extend, their extensions are constrained and their glycoprotein filaments remain covered by aqueous material. This was also the case during the first extension phase of the individual droplets that we examined. However, as extension progressed, the aqueous layer was progresses disrupted, exposing the glycoprotein. During the first extension phase E ranged from 0.00003 GPa, a value similar to that of fibronectin, a glycoprotein that anchors cells in the extracellular matrix, to 0.00292 GPa, a value similar to that of resilin in insect ligaments. Second phase E increased 4.7 - 19.4-fold. When compared at the same humidity the E of each species' glycoprotein was less than 5% of the value reported for its flagelliform fibers. This difference may facilitate the coordinated extension of these two capture thread components that is responsible for summing the thread's adhesive forces.en
dc.description.notesNational Science Foundation grant IOS-1257719 (BO) supported this study. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en
dc.description.sponsorshipNational Science Foundation grant [IOS-1257719]en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0196972en
dc.identifier.eissn1932-6203en
dc.identifier.issue5en
dc.identifier.othere0196972en
dc.identifier.pmid29847578en
dc.identifier.urihttp://hdl.handle.net/10919/89741en
dc.identifier.volume13en
dc.language.isoenen
dc.publisherPLOSen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleElastic modulus and toughness of orb spider glycoprotein glueen
dc.title.serialPLOS ONEen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.dcmitypeStillImageen

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