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SUMMARY:IMX Talks - Biological fabrication of hierarchically structured ma
 terials from protein condensates
DTSTART:20240621T110000
DTEND:20240621T120000
DTSTAMP:20260922T040559Z
UID:f846215c2d52b465ee35abc9303241166b976ed38a272f0c30ae4ef6
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Matthew J. Harrington\, McGill University\, Montreal\, Q
 uebec\, Canada\nNature provides an important role model for inspiring
  sustainable production of high-performance polymeric materials. For exam
 ple\, mussels rapidly fabricate hierarchically structured biopolymeric 
 fibersknown as byssal threads\, which have emerged as an important source
  of bio-inspiration due to theirremarkable material properties (e.g.\, 
 high toughness\, self-healing\, wet adhesion). Understanding the physica
 l and chemical principles underlying byssal thread production may inspire
  greener materials fabrication in the future\; however\, currently\, 
 these design principles must first be elucidated. \n\nByssal threads ar
 e produced via bottom-up self-assembly of over 15 different protein bu
 ilding blocks\, which localize in specific regions of the fiber with nanos
 cale precision. The threads themselves consist of different functional re
 gions including an underwater glue\, a self-healing fiber\, an abrasion-re
 sistant flexible coating\, and a quick-release biointerface. Our group 
 has harnessed advanced material characterization techniques\, including 
 confocal Raman spectroscopy\, X-ray fluorescence microscopy and focused 
 ion beam scanning electron microscopy (FIB-SEM)\, coupled with traditi
 onal biochemical approaches to investigate the fabrication of these diff
 erent components. We have discovered that mussels employ secretory vesi
 cles filled with condensed fluid protein phases (e.g.\, coacervates\, li
 quid crystals) as precursors for byssus assembly. These dynamic fluid 
 phases enable the pre-organization of protein building blocks\, which re
 spond to specific chemical and physical triggers (pH\, redox potential\,
  ion content\, mechanical shear) to initiate the “fluid-to-solid” t
 ransformation. In the adhesive\, protein condensates are secreted into a 
 network of channels resembling a microfluidic device\, where they underg
 oliquid-liquid phase separation (LLPS) and are simultaneously cross-lin
 ked via coordination complexation with co-secreted metal ions (Fe and
  V). Extracted design principles hold direct relevance for inspiring p
 roduction of advanced polymeric materials and adhesives.
LOCATION:MXF 312 https://plan.epfl.ch/?room==MXF%20312
STATUS:CONFIRMED
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