Nediljko Budisa

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Nediljko "Ned" Budisa
Nediljko Budisa 2012.jpg
Ned in a TU Berlin Laboratory in 2012
Born (1966-11-21) 21 November 1966 (age 58)
Nationality Croatian
Alma mater Faculty of Science, University of Zagreb
Scientific career
Fields Biochemistry, bioorganic chemistry, synthetic biology
Institutions University of Manitoba

Nediljko "Ned" Budisa (Croatian : Nediljko Budiša; born 21 November 1966) is a Croatian biochemist, professor and holder of the Tier 1 Canada Research Chair (CRC) for chemical synthetic biology at the University of Manitoba. As pioneer in the areas of genetic code engineering and chemical synthetic biology (Xenobiology), his research has a wide range of applications in biotechnology and engineering biology in general. Being highly interdisciplinary, it includes bioorganic and medical chemistry, structural biology, biophysics and molecular biotechnology as well as metabolic and biomaterial engineering. He is the author of the only textbook in his research field: “Engineering the genetic code: expanding the amino acid repertoire for the design of novel proteins”. [1]

Contents

Early life, education and career

Ned Budisa earned a High school teacher diploma in Chemistry and Biology in 1990, a B.S. in Molecular Biology and MSc in Biophysics in 1993 from the University of Zagreb. He received a PhD in 1997 from the Technical University of Munich where his thesis advisor was Professor Robert Huber. He also habilitated at the Technical University of Munich in 2005 and worked afterwards as a junior group leader ("Molecular Biotechnology") [2] at the Max Planck Institute for Biochemistry in Munich. Between 2007 and 2010 he was a member of CIPSM in Munich. [3] He was appointed as full professor of biocatalysis at the TU Berlin in 2010 [4] until the end of 2018, when he accepted the Tier 1 CRC position in Chemical Synthetic Biology at the University of Manitoba. [5] Ned Budisa is also a member of the Excellence Cluster ‘Unifying Systems in Catalysis’ (UniSysCat) [6] and keeps adjunct professor status at the TU Berlin. In 2014, he founded the first Berlin iGEM team. [7]

Research

Ned Budisa applies the Selective Pressure Incorporation (SPI) method [8] that enables single and multiple [9] in vivo incorporations of synthetic (i.e. non-canonical) amino acid analogs in proteins, preferably by sense codon reassignment. [10] His methodology allows for fine chemical manipulations of the amino acid side chains, mainly of proline, tryptophan and methionine. These experiments are often assisted with simple metabolic engineering. [11] [12] Ned's research goal is the transfer of various physicochemical properties and bioorthogonal chemistry reactions (chemoselective ligations such as click chemistry) as well as special spectroscopic features (e.g. blue [13] and golden [14] fluorescence or vibration energy transfer [15] ) into the proteins of living cells. In addition, his method allows the delivery of element-specific properties (fluorine, selenium and tellurium) into the biochemistry of life. [16]

Ned Budisa is well known for the establishment of the use of selenium-containing non-canonical amino acids for protein X-ray crystallography [17] and fluorine-containing analogs for 19F NMR-spectroscopy and protein folding studies. [18] He was the first to demonstrate the use of genetic code engineering as a tool for the creation of therapeutic proteins [19] and ribosomally synthesized peptide-drugs. [20] He has succeeded with innovative engineering of biomaterials, in particular photoactivatable mussel-based underwater adhesives. [21] Ned Budisa made seminal contributions to our understanding of the role of methionine oxidation in prion protein aggregation [22] and has discovered the roles of proline side chain conformations (endo-exo isomerism) in translation, folding and stability of proteins. [23] [24]

Together with his co-worker Vladimir Kubyshkin, the new-to-nature hydrophobic [25] polyproline-II helix foldamer was designed. Along with Budisa's previous work on bioexpression using proline analogues, the results of this project contributed to the establishment of the Alanine World hypothesis. [26] It explains why nature chose the genetic code [27] with "only" 20 canonical amino acids for ribosomal protein synthesis. [28]

In 2015, the team led by Ned Budisa reported the successful completion of a long-term evolution experiment that resulted in full, proteome-wide substitution of all 20,899 tryptophan residues with thienopyrrole-alanine in the genetic code of the bacterium Escherichia coli. [29] This is a solid basis for the evolution of life with alternative building blocks, foldamers or biochemistries. [30] At the same time, this approach might be an interesting biosafety technology to evolve biocontained synthetic cells [31] equipped with a "genetic firewall" which prevents their survival outside of man-made unnatural environments. [32] Similar experiments with fluorinated tryptophan analogs [33] as xenobiotic compounds (in collaboration with Beate Koksch from the Free University of Berlin) has led to the discovery of exceptional physiological plasticity in microbial cultures during adaptive laboratory evolution, making them potential environmentally friendly tools for new bioremediation strategies.

Ned Budisa is also actively involved in the debate of possible societal, ethical and philosophical impacts of radical genetic code engineering in the context of synthetic cells and life as well as technologies derived thereof. [34]

Awards and honors (selection)

See also

Related Research Articles

<span class="mw-page-title-main">Amino acid</span> Organic compounds containing amine and carboxylic groups

Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.

<span class="mw-page-title-main">Genetic code</span> Rules by which information encoded within genetic material is translated into proteins

The genetic code is the set of rules used by living cells to translate information encoded within genetic material into proteins. Translation is accomplished by the ribosome, which links proteinogenic amino acids in an order specified by messenger RNA (mRNA), using transfer RNA (tRNA) molecules to carry amino acids and to read the mRNA three nucleotides at a time. The genetic code is highly similar among all organisms and can be expressed in a simple table with 64 entries.

<span class="mw-page-title-main">Cysteine</span> Proteinogenic amino acid

Cysteine is a semiessential proteinogenic amino acid with the formula HOOC−CH(−NH2)−CH2−SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. L‑Cysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστη kýsti, "bladder".

<span class="mw-page-title-main">Pyrrolysine</span> Chemical compound

Pyrrolysine is an α-amino acid that is used in the biosynthesis of proteins in some methanogenic archaea and bacteria; it is not present in humans. It contains an α-amino group and a carboxylic acid group. Its pyrroline side-chain is similar to that of lysine in being basic and positively charged at neutral pH.

<span class="mw-page-title-main">Alanine</span> Α-amino acid that is used in the biosynthesis of proteins

Alanine, or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently it is classified as a nonpolar, aliphatic α-amino acid. Under biological conditions, it exists in its zwitterionic form with its amine group protonated and its carboxyl group deprotonated. It is non-essential to humans as it can be synthesized metabolically and does not need to be present in the diet. It is encoded by all codons starting with GC.

<span class="mw-page-title-main">Synthetic biology</span> Interdisciplinary branch of biology and engineering

Synthetic biology (SynBio) is a multidisciplinary field of science that focuses on living systems and organisms, and it applies engineering principles to develop new biological parts, devices, and systems or to redesign existing systems found in nature.

<span class="mw-page-title-main">Auxotrophy</span> Inability to synthesize an organic compound required for growth

Auxotrophy is the inability of an organism to synthesize a particular organic compound required for its growth. An auxotroph is an organism that displays this characteristic; auxotrophic is the corresponding adjective. Auxotrophy is the opposite of prototrophy, which is characterized by the ability to synthesize all the compounds needed for growth.

<span class="mw-page-title-main">Supramolecular chemistry</span> Branch of chemistry

Supramolecular chemistry refers to the branch of chemistry concerning chemical systems composed of a discrete number of molecules. The strength of the forces responsible for spatial organization of the system range from weak intermolecular forces, electrostatic charge, or hydrogen bonding to strong covalent bonding, provided that the electronic coupling strength remains small relative to the energy parameters of the component. While traditional chemistry concentrates on the covalent bond, supramolecular chemistry examines the weaker and reversible non-covalent interactions between molecules. These forces include hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, pi–pi interactions and electrostatic effects.

Xenobiology (XB) is a subfield of synthetic biology, the study of synthesizing and manipulating biological devices and systems. The name "xenobiology" derives from the Greek word xenos, which means "stranger, alien". Xenobiology is a form of biology that is not (yet) familiar to science and is not found in nature. In practice, it describes novel biological systems and biochemistries that differ from the canonical DNA–RNA-20 amino acid system. For example, instead of DNA or RNA, XB explores nucleic acid analogues, termed xeno nucleic acid (XNA) as information carriers. It also focuses on an expanded genetic code and the incorporation of non-proteinogenic amino acids, or “xeno amino acids” into proteins.

<span class="mw-page-title-main">Molecular knot</span> Molecule whose structure resembles a knot

In chemistry, a molecular knot is a mechanically interlocked molecular architecture that is analogous to a macroscopic knot. Naturally-forming molecular knots are found in organic molecules like DNA, RNA, and proteins. It is not certain that naturally occurring knots are evolutionarily advantageous to nucleic acids or proteins, though knotting is thought to play a role in the structure, stability, and function of knotted biological molecules. The mechanism by which knots naturally form in molecules, and the mechanism by which a molecule is stabilized or improved by knotting, is ambiguous. The study of molecular knots involves the formation and applications of both naturally occurring and chemically synthesized molecular knots. Applying chemical topology and knot theory to molecular knots allows biologists to better understand the structures and synthesis of knotted organic molecules.

<span class="mw-page-title-main">Chemical biology</span> Scientific discipline

Chemical biology is a scientific discipline between the fields of chemistry and biology. The discipline involves the application of chemical techniques, analysis, and often small molecules produced through synthetic chemistry, to the study and manipulation of biological systems. Although often confused with biochemistry, which studies the chemistry of biomolecules and regulation of biochemical pathways within and between cells, chemical biology remains distinct by focusing on the application of chemical tools to address biological questions.

Click chemistry is an approach to chemical synthesis that emphasizes efficiency, simplicity, selectivity, and modularity in chemical processes used to join molecular building blocks. It includes both the development and use of "click reactions", a set of simple, biocompatible chemical reactions that meet specific criteria like high yield, fast reaction rates, and minimal byproducts. It was first fully described by K. Barry Sharpless, Hartmuth C. Kolb, and M. G. Finn of The Scripps Research Institute in 2001. In this seminal paper, Sharpless argued that synthetic chemistry could emulate the way nature constructs complex molecules, using efficient reactions to join together simple, non-toxic building blocks.

<span class="mw-page-title-main">Directed evolution</span> Protein engineering method

Directed evolution (DE) is a method used in protein engineering that mimics the process of natural selection to steer proteins or nucleic acids toward a user-defined goal. It consists of subjecting a gene to iterative rounds of mutagenesis, selection and amplification. It can be performed in vivo, or in vitro. Directed evolution is used both for protein engineering as an alternative to rationally designing modified proteins, as well as for experimental evolution studies of fundamental evolutionary principles in a controlled, laboratory environment.

<span class="mw-page-title-main">Bioconjugation</span> Chemical process

Bioconjugation is a chemical strategy to form a stable covalent link between two molecules, at least one of which is a biomolecule. Methods to conjugate biomolecules are applied in various field, including medicine, diagnostics, biocatalysis and materials. Synthetically modified biomolecules can have diverse functionalities, such as tracking cellular events, revealing enzyme function, determining protein biodistribution, imaging specific biomarkers, and delivering drugs to targeted cells.

<span class="mw-page-title-main">Expanded genetic code</span> Modified genetic code

An expanded genetic code is an artificially modified genetic code in which one or more specific codons have been re-allocated to encode an amino acid that is not among the 22 common naturally-encoded proteinogenic amino acids.

An alloprotein is a novel synthetic protein containing one or more "non-natural" amino acids. Non-natural in the context means an amino acid either not occurring in nature, or occurring in nature but not naturally occurring within proteins.

<span class="mw-page-title-main">Photoactivated peptide</span>

Photoactivated peptides are modified natural or synthetic peptides whose functions can be activated or controlled using light. These peptides incorporate light-sensitive elements that allow for precise regulation their biological activity in both space and time. The activation can be either irreversible, as in the case of caged peptides with photocleavable protecting groups, or reversible, utilizing molecular photoswitches like azobenzenes or diarylethenes, and diarylethenes By incorporating these light-responsive components into the peptide structure, peptide properties, functions, and biological activities can be manipulated with high precision. This approach enables targeted activation of peptides in specific areas, making photoactivated peptides valuable tools for applications in cancer therapy, drug delivery, and probing molecular interactions in living cells and in organisms.

An artificial metalloenzyme (ArM) is a designer metalloprotein, not found in nature, which can catalyze desired chemical reactions. Despite fitting into classical enzyme categories, ArMs also have potential in new-to-nature chemical reactivity like catalysing Suzuki coupling, Metathesis etc., which were never reported among natural enzymatic reactions.

<span class="mw-page-title-main">Luis Moroder</span> Italian chemist (1940–2024)

Luis Moroder was an Italian peptide chemist, who pioneered research on the interactions between peptide hormones and cell membrane-bound hormone receptors. He later expanded this research to other biological systems of medical relevance such as protein inhibitors, collagens, and synthetic proteins. A hallmark of his research is interdisciplinarity as reflected in his use and development of methods in organic chemistry, biophysics and molecular biology. He was a co-editor of the five-volume Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics. From 2008 he was the editor-in-chief of the Journal of Peptide Science, the official journal of the European Peptide Society.

<span class="mw-page-title-main">Jason Micklefield</span> British Biochemist

Jason Micklefield is a British Biochemist and a professor in the Department of Chemistry at The University of Manchester. His research involves the discovery, characterisation and engineering of biosynthetic pathways to new bioactive natural products, particularly antibiotics. He is also interested in the discovery, structure, mechanism and engineering of enzymes for synthetic applications, including the integration of enzymes with chemocatalysis for telescoping routes to pharmaceuticals and other valuable products.

References

  1. Budisa, Nediljko (2005). The book at the Wiley Online Library. doi:10.1002/3527607188. ISBN   9783527312436.
  2. "Molecular Biotechnology". Max Planck Institute. Archived from the original on June 10, 2007. Retrieved August 10, 2017.
  3. "List of CIPSM professors" . Retrieved August 10, 2017.
  4. "Website of the Biocatalysis group" . Retrieved August 10, 2017.
  5. "University of Manitoba welcoming Ned Budisa". October 16, 2018. Retrieved August 17, 2019.
  6. "UniSysCat Cluster of Excellence" . Retrieved August 17, 2019.
  7. "iGEM team Berlin" . Retrieved August 10, 2017.
  8. Budisa, N. (2004). "Prolegomena to future efforts on genetic code engineering by expanding its amino acid repertoire". Angewandte Chemie International Edition. 43: 3387–3428. doi:10.1002/anie.20030064 (inactive November 1, 2024).{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link)
  9. Lepthien, S.; Merkel, L.; Budisa, N. (2010). "In Vivo Double and Triple Labeling of Proteins Using Synthetic Amino Acids". Angewandte Chemie International Edition. 49 (32): 5446–5450. doi:10.1002/anie.201000439. PMID   20575122.
  10. Bohlke, N.; Budisa, N. (2014). "Sense codon emancipation for proteome-wide incorporation of noncanonical amino acids: rare isoleucine codon AUA as a target for genetic code expansion". FEMS Microbiology Letters. 351 (2): 133–44. doi:10.1111/1574-6968.12371. PMC   4237120 . PMID   24433543. S2CID   5735708.
  11. Völler, J.-S.; Budisa, N. (2017). "Coupling genetic code expansion and metabolic engineering for synthetic cells". Current Opinion in Biotechnology. 48: 1–7. doi:10.1016/j.copbio.2017.02.002. PMID   28237511.
  12. Exner, M. P.; Kuenzl, S.; Schwagerus, S.; To, T.; Ouyang, Z.; Hoesl, M. G.; Lensen, M. C.; Hackenberger, C. P. R.; Panke, S.; Budisa, N. (2017). "Design of an S-Allylcysteine in situ production and incorporation system based on a novel pyrrolysyl-tRNA synthetase variant". ChemBioChem. 18 (1): 85–90. doi:10.1002/cbic.201600537. PMID   27862817. S2CID   23006925.
  13. Lepthien, S.; Hoesl, M. G.; Merkel, L.; Budisa, N. (2008). "Azatryptophans endow proteins with intrinsic blue fluorescence". Proc. Natl. Acad. Sci. USA. 105 (42): 16095–16100. Bibcode:2008PNAS..10516095L. doi: 10.1073/pnas.0802804105 . PMC   2571030 . PMID   18854410.
  14. Bae, J.; Rubini, M.; Jung, G.; Wiegand, G.; Seifert, M. H. J.; Azim, M. K.; Kim, J. S.; Zumbusch, A.; Holak, T. A.; Moroder, L.; Huber, R.; Budisa, N. (2003). "Expansion of the Genetic Code Enables Design of a Novel "Gold" Class of Green Fluorescent Proteins". Journal of Molecular Biology. 328 (5): 977–1202. doi:10.1016/s0022-2836(03)00364-4. PMID   12729742.
  15. Baumann, T.; Hauf, M.; Schildhauer, F.; Eberl, K.; Durkin, P. M.; Deniz, E.; Löffler, J. G.; Acevedo-Rocha, C. G.; Jaric, J.; Martins, B. M.; Dobbek, H.; Bredenbeck, J.; Budisa, N. (2019). "Site-Resolved Observation of Vibrational Energy Transfer Using a Genetically Encoded Ultrafast Heater". Angewandte Chemie International Edition. 58 (9): 2527–2903. doi:10.1002/anie.201812995. PMID   30589180. S2CID   58584644.
  16. Agostini, F.; Völler, J-S.; Koksch, B.; Acevedo-Rocha, C. G.; Kubyshkin, V.; Budisa, N. (2017). "Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology". Angewandte Chemie International Edition. 56 (33): 9680–9703. doi:10.1002/anie.201610129. PMID   28085996.
  17. Budisa, N.; Steipe, B.; Demange, P.; Eckerskorn, C.; Kellermann, J.; Huber, R. (1995). "High level biosynthetic substitution of methionine in proteins by its analogues 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli". Eur. J. Biochem. 230 (2): 788–796. doi:10.1111/j.1432-1033.1995.0788h.x. PMID   7607253.
  18. Seifert, M. H.; Ksiazek, D.; Smialowski, P.; Azim, M. K.; Budisa, N.; Holak, T. A. (2002). "Slow Conformational Exchange Processes in Green Fluorescent Protein Variants evidenced by NMR Spectroscopy". J. Am. Chem. Soc. 124 (27): 7932–7942. doi:10.1021/ja0257725. PMID   12095337.
  19. Budisa, N.; Minks, C.; Medrano, F. J.; Lutz, J.; Huber, R.; Moroder, L. (1998). "Residue specific bioincorporation of non-natural biologically active amino acids into proteins as possible drug carriers. Structure and stability of per-thiaproline mutant or annexin V". Proc. Natl. Acad. Sci. USA. 95 (2): 455–459. doi: 10.1073/pnas.95.2.455 . PMC   18441 . PMID   9435213.
  20. Budisa, N. (2013). "Expanded genetic code for the engineering of ribosomally synthetized[sic] and post-translationally modified peptide natural products (RiPPs)". Current Opinion in Biotechnology. 24 (4): 591–598. doi:10.1016/j.copbio.2013.02.026. PMID   23537814.
  21. Hauf, M.; Richter, F.; Schneider, T.; Faidt, T.; Martins, B. M.; Baumann, T.; Durkin, P.; Dobbek, H.; Jacobs, K.; Moeglich, A.; Budisa, N. (2017). "Photoactivatable mussel-based underwater adhesive proteins by an expanded genetic code". ChemBioChem. 18 (18): 1819–1823. doi:10.1002/cbic.201700327. PMID   28650092. S2CID   4919816.
  22. Wolschner, C.; Giese, A.; Kretzschmar, H.; Huber, R.; Moroder, L.; Budisa, N. (2009). "Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein". Proc. Natl. Acad. Sci. USA. 106 (19): 7756–7761. Bibcode:2009PNAS..106.7756W. doi: 10.1073/pnas.0902688106 . PMC   2674404 . PMID   19416900.
  23. Steiner, T.; Hess, P.; Bae, J. H.; Moroder, L.; Budisa, N. (2008). "Synthetic Biology of Proteins: Tuning GFP´s Folding and Stability with Fluoroproline". PLOS ONE. 3 (2): e1680. Bibcode:2008PLoSO...3.1680S. doi: 10.1371/journal.pone.0001680 . PMC   2243022 . PMID   18301757. S2CID   10089602.
  24. Doerfel, L. K.; Wohlgemuth, I.; Kubyshkin, V.; Starosta, A. L.; Wilson, D. N.; Budisa, N. (2015). "Entropic Contribution of Elongation Factor P to Proline Positioning at the Catalytic Center of the Ribosome". J. Am. Chem. Soc. 137 (40): 12997–13006. doi:10.1021/jacs.5b07427. hdl:11858/00-001M-0000-0028-E3C7-1. PMID   26384033.
  25. Kubyshkin, V.; Grage, S. L.; Bürck, J.; Ulrich, A. S.; Budisa, N. (2018). "Transmembrane Polyproline Helix". J. Phys. Chem. Lett. 9 (9): 2170–2174. doi:10.1021/acs.jpclett.8b00829. PMID   29638132.
  26. Kubyshkin, V.; Budisa, N. (2019). "Anticipating alien cells with alternative genetic codes: away from the alanine world!". Current Opinion in Biotechnology. 60: 242–249. doi: 10.1016/j.copbio.2019.05.006 . PMID   31279217. S2CID   195820138.
  27. Kubyshkin, V.; Acevedo-Rocha, C. G.; Budisa, N. (2017). "On universal coding events in protein biogenesis". Biosystems. 164: 16–25. doi: 10.1016/j.biosystems.2017.10.004 . PMID   29030023.
  28. Kubyshkin, V.; Budisa, N. (2019). "The Alanine World Model for the Development of the Amino Acid Repertoire in Protein Biosynthesis". Int. J. Mol. Sci. 20 (21): 5507. doi: 10.3390/ijms20215507 . PMC   6862034 . PMID   31694194. S2CID   207936069.
  29. Hoesl, M. G.; Oehm, S.; Durkin, P.; Darmon, E.; Peil, L.; Aerni, H.-R.; Rappsilber, J.; Rinehart, J.; Leach, D.; Söll, D.; Budisa, N. (2015). "Chemical evolution of a bacterial proteome". Angewandte Chemie International Edition. 54 (34): 10030–10034. doi:10.1002/anie.201502868. PMC   4782924 . PMID   26136259. NIHMSID: NIHMS711205
  30. Kubyshkin, V.; Budisa, N. (2017). "Synthetic alienation of microbial organisms by using genetic code engineering: Why and how?". Biotechnology Journal. 12 (8): 1600097. doi:10.1002/biot.201600097. PMID   28671771.
  31. Diwo, C.; Budisa, N. (2019). "Alternative Biochemistries for Alien Life: Basic Concepts and Requirements for the Design of a Robust Biocontainment System in Genetic Isolation". Genes. 10 (1): 17. doi: 10.3390/genes10010017 . PMC   6356944 . PMID   30597824. S2CID   58570773.
  32. Acevedo-Rocha, C. G.; Budisa, N. (2011). "On the Road towards Chemically Modified Organisms Endowed with a Genetic Firewall". Angewandte Chemie International Edition. 50 (31): 6960–6962. doi:10.1002/anie.201103010. PMID   21710510.
  33. Agostini, F.; Sinn, L.; Petras, D.; Schipp, C. J.; Kubyshikin, V; Berger, A. A.; Dorrestein, P. C; Rappsilber, J.; Budisa, N.; Koksch, B. (2019). "Laboratory evolution of Escherichia coli enables life based on fluorinated amino acids". bioRxiv   10.1101/665950 .
  34. Schmidt, M.; Pei, L.; Budisa, N. (2018). Xenobiology: State-of-the-art, Ethics and Philosophy of new-to-nature organisms. Vol. 162. pp. 301–315. doi:10.1007/10_2016_14. ISBN   978-3-319-55317-7. ISSN   0724-6145. PMID   28567486.{{cite book}}: |journal= ignored (help)
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