Molecular design of performance proteins with repetitive sequences: recombinant flagelliform spider silk as basis for biomaterials.
Most performance proteins responsible for the mechanical stability of cells and organisms reveal highly repetitive sequences. Mimicking such performance proteins is of high interest for the design of nanostructured biomaterials. In this article, flagelliform silk is exemplary introduced to describe a general principle for designing genes of repetitive performance proteins for recombinant expression in Escherichia coli . In the first step, repeating amino acid sequence motifs are reversely transcripted into DNA cassettes, which can in a second step be seamlessly ligated, yielding a designed gene. Recombinant expression thereof leads to proteins mimicking the natural ones. The recombinant proteins can be assembled into nanostructured materials in a controlled manner, allowing their use in several applications.
Vendrely
Charlotte
C
TUM, Department Chemie, Lehrstuhl Biotechnologie, Garching, Germany.
Ackerschott
Christian
C
Römer
Lin
L
Scheibel
Thomas
T
D020816:Amino Acid Motifs / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005813:Genes, Synthetic; D049329:Nanostructures; D036103:Nanotechnology / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid / Q000235:genetics; D047011:Silk / Q000096:biosynthesis* / Q000235:genetics
D011994:Recombinant Proteins; D047011:Silk