Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
ACS Synth Biol ; 9(12): 3388-3399, 2020 12 18.
Article in English | MEDLINE | ID: mdl-33201684

ABSTRACT

Structural proteins such as "suckerins" present promising avenues for fabricating functional materials. Suckerins are a family of naturally occurring block copolymer-type proteins that comprise the sucker ring teeth of cephalopods and are known to self-assemble into supramolecular networks of nanoconfined ß-sheets. Here, we report the characterization and controllable, nanoscale self-assembly of suckerin-12 (S12). We characterize the impacts of salt, pH, and protein concentration on S12 solubility, secondary structure, and self-assembly. In doing so, we identify conditions for fabricating ∼100 nm nanoassemblies (NAs) with narrow size distributions. Finally, by installing a noncanonical amino acid (ncAA) into S12, we demonstrate the assembly of NAs that are covalently conjugated with a hydrophobic fluorophore and the ability to change self-assembly and ß-sheet content by PEGylation. This work presents new insights into the biochemistry of suckerin-12 and demonstrates how ncAAs can be used to expedite and fine-tune the design of protein materials.


Subject(s)
Nanotechnology , Proteins/metabolism , Animals , Cycloaddition Reaction , Decapodiformes/metabolism , Escherichia coli/metabolism , Hydrogen-Ion Concentration , Phenylalanine/genetics , Phenylalanine/metabolism , Point Mutation , Protein Conformation, beta-Strand , Protein Folding , Proteins/chemistry , Proteins/genetics , Recombinant Proteins/biosynthesis , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification , Salts/chemistry , Solubility
SELECTION OF CITATIONS
SEARCH DETAIL
...