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SUMMARY:Using Proteins to Prepare Functional Polymeric Nanomaterials - Pro
 f. Nico Bruns\, Adolphe Merkle Institute\, University of Fribourg\, Switze
 rland
DTSTART:20160512T100000Z
DTEND:20160512T110000Z
UID:TALK66226@talks.cam.ac.uk
CONTACT:Sharon Connor
DESCRIPTION:Proteins are fascinating macromolecules. Nature evolved ways t
 o accurately control the monomer sequence\, making them the ultimate preci
 sion polymers. Proteins fold and self-assemble into well-defined three dim
 ensional nanoobjects. Moreover\, enzymes efficiently catalyze numerous che
 mical reactions with high selectivity at mild reaction conditions. Compare
 d to the properties and functions of nature’s macromolecules\, even the 
 most sophisticated synthetic polymers still appear to be simple and only o
 ffer comparably basic functionality. Therefore\, an interdisciplinary appr
 oach combining polymer chemistry and protein science creates new opportuni
 ties to design and realize functional materials\, as well as to support th
 e environmentally friendly synthesis of polymers.\n\nThe protein cage ther
 mosome is a hollow nanosphere with gated pores that are so large that macr
 omolecules can diffuse in and out of the cage. By site-directed mutagenesi
 s and chemical conjugation a variety of guests were entrapped into this ca
 ge. Thus\, thermosome-polymer conjugates were developed into powerful deli
 very vehicles for small interfering RNA and are useful templates for the s
 ynthesis of nanoparticles. Moreover\, the thermosome was used as nanoreact
 or for the controlled synthesis of polymers in a confined reaction space. 
  A second approach to harness the functionality of proteins within synthet
 ic materials is to dope engineering materials with small quantities of pro
 teins. Fluorescent proteins are force-responsive and loose their fluoresce
 nce if mechanically perturbed. This effect was exploited to develop fiber-
 reinforced composites in which fluorescent proteins act as a mechanical se
 nsor on the nanoscale. Such self-reporting materials can detect and report
  micro damage and could find application as safety feature to avoid catast
 rophic material failure of load-bearing components. In a third example\, t
 he opportunities that arise from enzymatic polymerizations will be highlig
 hted. Our group discovered that some metalloproteins such as horseradish p
 eroxidase and hemoglobin can catalyze atom transfer radical polymerization
 s (ATRP). This novel enzymatic activity allows to prepare well-defined pol
 ymers that are otherwise not accessible through classic ATRP. Moreover\, t
 he controlled synthesis of polymer brushes on surfaces can be tuned in uni
 que ways and polymer-filled polymersomes can be prepared by confining the 
 polymerization into polymer vesicles.\n
LOCATION:Pfizer Lecture Theatre\,  Department of Chemistry
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