Loading…

Photoactivatable Mussel‐Based Underwater Adhesive Proteins by an Expanded Genetic Code

Marine mussels exhibit potent underwater adhesion abilities under hostile conditions by employing 3,4‐dihydroxyphenylalanine (DOPA)‐rich mussel adhesive proteins (MAPs). However, their recombinant production is a major biotechnological challenge. Herein, a novel strategy based on genetic code expans...

Full description

Saved in:
Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2017-09, Vol.18 (18), p.1819-1823
Main Authors: Hauf, Matthias, Richter, Florian, Schneider, Tobias, Faidt, Thomas, Martins, Berta M., Baumann, Tobias, Durkin, Patrick, Dobbek, Holger, Jacobs, Karin, Möglich, Andreas, Budisa, Nediljko
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Marine mussels exhibit potent underwater adhesion abilities under hostile conditions by employing 3,4‐dihydroxyphenylalanine (DOPA)‐rich mussel adhesive proteins (MAPs). However, their recombinant production is a major biotechnological challenge. Herein, a novel strategy based on genetic code expansion has been developed by engineering efficient aminoacyl‐transfer RNA synthetases (aaRSs) for the photocaged noncanonical amino acid ortho‐nitrobenzyl DOPA (ONB‐DOPA). The engineered ONB‐DOPARS enables in vivo production of MAP type 5 site‐specifically equipped with multiple instances of ONB‐DOPA to yield photocaged, spatiotemporally controlled underwater adhesives. Upon exposure to UV light, these proteins feature elevated wet adhesion properties. This concept offers new perspectives for the production of recombinant bioadhesives. Light‐controllable biomimetic glue: Expansion of the genetic code with the noncanonical amino acid (ncAA) ortho‐nitrobenzyl 3,4‐dihydroxyphenylalanine (ONB‐DOPA) allows the production of photoactivatable mussel adhesive proteins in vivo. Carrying the ncAA at multiple sites, these proteins show spatiotemporally controllable adhesive properties.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201700327