title: Bioengineered chimeric spider silk-uranium binding proteins.
abstract: Heavy metals constitute a source of environmental pollution. Here, novel functional hybrid biomaterials for specific interactions with heavy metals are designed by bioengineering consensus sequence repeats from spider silk of Nephila clavipes with repeats of a uranium peptide recognition motif from a mutated 33-residue of calmodulin protein from Paramecium tetraurelia. The self-assembly features of the silk to control nanoscale organic/inorganic material interfaces provides new biomaterials for uranium recovery. With subsequent enzymatic digestion of the silk to concentrate the sequestered metals, options can be envisaged to use these new chimeric protein systems in environmental engineering, including to remediate environments contaminated by uranium.
authors.affiliation: Department of Chemistry, Tufts University, Medford, MA 02155, USA.
authors.forename: Sreevidhya Tarakkad
authors.initials: ST
authors.lastname: Krishnaji
authors.forename: David L
authors.initials: DL
authors.lastname: Kaplan
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D060829:Arthropod Proteins / Q000235:genetics* / Q000378:metabolism*; D002942:Circular Dichroism; D004785:Environmental Pollutants / Q000378:metabolism; D005453:Fluorescence; D019216:Metals, Heavy / Q000737:chemistry / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D014501:Uranium / Q000378:metabolism*
chemical_list: D060829:Arthropod Proteins; D004785:Environmental Pollutants; D019216:Metals, Heavy; D011993:Recombinant Fusion Proteins; D014501:Uranium