Congeneric bio-adhesive mussel foot proteins designed by modified prolines revealed a chiral bias in unnatural translation

Biochemical and Biophysical Research Communications

Volumn 421, Issue 4, 2012, Pages 646-650

  Larregola, Maud ^a   Moore, Shannon ^a   Budisa, Nediljko ^a  

^a TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Bio adhesive; Fluoroproline; Genetic code engineering; Hydroxyproline; Mussel foot protein

Indexed keywords

BIOMATERIAL; FLUOROPROLINE; HYDROXYL GROUP; HYDROXYPROLINE; MUSSEL ADHESIVE PROTEIN; PROLINE; PROLINE DERIVATIVE; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; CHIRALITY; IN VIVO STUDY; MUSSEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; RNA EDITING; RNA TRANSLATION; STEREOISOMERISM;

AMINO ACID SEQUENCE; ANIMALS; CELL ADHESION MOLECULES; MOLECULAR SEQUENCE DATA; MYTILUS; PROLINE; RECOMBINANT PROTEINS;

EID: 84861221005     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.031     Document Type: Article

References (28)

1. Stewart R.J., Ransom T.C., Hlady V. Natural underwater adhesives. J. Polym. Sci. Pol. Phys. 2011, 49:757-771.
2. Silverman H.G., Roberto F.F. Understanding marine mussel adhesion. Mar. Biotechnol. 2007, 9:661-681.
3. Wiegemann M. Adhesion in blue mussels (Mytilus edulis) and barnacles (genus Balanus): mechanisms and technical applications. Aquat. Sci. 2005, 67:166-176.
4. Hwang D.S., Gim Y., Yoo H.J., Cha H.J. Practical recombinant hybrid mussel bloadhesive fp-151. Biomaterials 2007, 28:3560-3568.
5. Budisa N. Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire. Angew. Chem. Int. Ed. 2004, 43:6426-6463.
6. Renner C., Alefelder S., Bae J.H., Budisa N., Huber R., Moroder L. Fluoroprolines as tools for protein design and engineering. Angew. Chem. Int. Ed. 2001, 40:923-925.
7. Wilker J.J. The iron-fortified adhesive system of marine mussels. Angew. Chem. Int. Ed. 2010, 49:8076-8078.
8. Harrington M.J., Masic A., Holten-Andersen N., Waite J.H., Fratzl P. Iron-clad fibers: a metal-based biological strategy for hard flexible coatings. Science 2010, 328:216-220.
9. Sun C.J., Waite J.H. Mapping chemical gradients within and along a fibrous structural tissue, mussel byssal threads. J. Biol. Chem. 2005, 280:39332-39336.
10. Budisa N. Engineering the Genetic Code 2005, Wiley-VCH Weinheim.
11. Holmgren S.K., Bretscher L.E., Taylor K.M., Raines R.T. A hyperstable collagen mimic. Chem. Biol. 1999, 6:63-70.
12. Neil E., Marsh G. Towards the nonstick egg: designing fluorous proteins. Chem. Biol. 2000, 7:R153-157.
13. Budisa N., Steipe B., Demange P., Eckerskorn C., Kellermann J., Huber R. High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 1995, 230:788-796.
14. Pesic A., Henkel M., Sussmuth R.D. Identification of the amino acid labionin and its desulfurised derivative in the type-III lantibiotic LabA2 by means of GC/MS. Chem. Commun. 2011, 47:7401-7403.
15. T. Steiner, P. Hess, J.H. Bae, B. Wiltschi, L. Moroder, N. Budisa, Synthetic Biology of Proteins: Tuning GFPs Folding and Stability with Fluoroproline, PLoS One 3 (2008).
16. Budisa N., et al. Residue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: Structure and stability of the per-thiaproline mutant of annexin V. Proc. Natl. Acad. Sci. USA 1998, 95:455-459.
17. Hoesl M.G., Acevedo-Rocha C.G., Nehring S., Royter M., Wolschner C., Wiltschi B., Budisa N., Antranikian G. Lipase congeners designed by genetic code engineering. Chem. Cat. Chem. 2011, 3:213-221.
18. Kim W.Y., George A., Evans M., Conticello V.P. Cotranslational incorporation of a structurally diverse series of proline analogues in an Escherichia coli expression system. Chem. Bio. Chem. 2004, 5:928-936.
19. Buechter D.D., Paolella D.N., Leslie B.S., Brown M.S., Mehos K.A., Gruskin E.A. Co-translational incorporation of Trans-4-hydroxyproline into recombinant proteins in bacteria. J. Biol. Chem. 2003, 278:645-650.
20. Shoulders M.D., Satyshur K.A., Forest K.T., Raines R.T. Stereoelectronic and steric effects in side chains preorganize a protein main chain. Proc. Natl. Acad. Sci. USA 2010, 107:559-564.
21. Kanyalkar M., Srivastava S., Coutinho E. Conformation of a model peptide of the tandem repeat decapeptide in mussel adhesive protein by NMR and MD simulations. Biomaterials 2002, 23:389-396.
22. Jenkins C.L., Raines R.T. Insights on the conformational stability of collagen. Nat. Prod. Rep. 2002, 19:49-59.
23. Patzold R., Schieber A., Bruckner H. Gas-chromatographic quantification of free d-amino acids in higher vertebrates. Biomed. Chromatogr. 2005, 19:466-473.
24. Liu C.C., Schultz P.G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 2010, 79:413-444.
25. Wang K.H., Neumann H., Peak-Chew S.Y., Chin J.W. Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion. Nat. Biotechnol. 2007, 25:770-777.
26. Lepthien S., Merkel L., Budisa N. In vivo double and triple labeling of proteins using synthetic amino acids. Angew. Chem. Int. Ed. 2010, 49:5446-5450.
27. Merkel L., Schauer M., Antranikian G., Budisa N. Parallel incorporation of different fluorinated amino acids: on the way to " teflon" proteins. Chem. Bio. Chem. 2010, 11:1505-1507.
28. Holzberger B., Marx A. Replacing 32 proline residues by a noncanonical amino acid results in a highly active DNA polymerase. J. Am. Chem. Soc. 2010, 132:15708-15713.