The academics presenting in the next Peptide and Protein Science online seminar will be Jack Jeffries, University College London, and Beate Koksch, Freie Universität Berlin.
Date: 04-04-2025
Time: 1:00-2:00 pm
Venue: online Zoom seminar
Registration: https://eu01web.zoom.us/meeting/register/u5Ikc-2grT4jH9326Nm6qwWzp1OMYDJlEU9e
Jack Jeffries, University College London
Mining the multitude: Cell free protein expression for metagenomic enzyme discovery
Cell free expression utilises the cellular transcriptional and translational machinery without the other cell processes such as growth and division for protein expression. It has found use in the production of proteins that may be toxic to a host cell, antimicrobial peptides, the screening of genetic parts or for the insertion of non-canonical/ non-natural amino acids. Due to the ability to scale down cell free expression systems and the short time frames needed for generation of quantifiable protein, we are interested in using it to explore the huge sequence space available from Metagenomes to identify candidates for industrial biocatalysis.
Beate Koksch, Freie Universität Berlin
Fluoropeptides as biodegradable biopolymers
Fluorine as a substituent causes drastic changes in the biophysical properties of organic molecules and polymers. This results in highly appreciated properties of drugs and materials that are ubiquitous in our everyday lives today. However, the unique stability of the C-F bond can be problematic if this leads to poor biodegradability. Combining the special material properties of fluoropolymers with the biocompatibility of peptides could be an attractive solution.
The incorporation of fluorine substituents into otherwise hydrophobic amino acid side chains induces a polarity that no other functionality can generate in this form. This special polarity leads to drastic changes in the biophysical properties of peptides in terms of hydrophobicity, lipophilicity, solubility as well as folding and proteolytic stability; criteria that are of utmost importance for biomolecular recognition, self-assembly and, thus, the properties of peptide-based biomaterials. [1] Generally, the combination of fluorine substituents, which lead to the much-described and widely used omniphobic properties in organic polymers, with the water-soluble properties of peptides (depending on their sequence and folding) promises new classes of compounds with extremely interesting properties. Fluoropeptides, which consist exclusively or to a large extent of fluorinated amino acids, offer a wide range of unexplored possibilities in terms of folding, self-assembly and material properties. We have recently taken the first steps into this uncharted scientific territory. [2, 3]
The lecture will present the first polyfluorinated peptides that consist of more than 50% of fluorinated amino acids. They represent an amphipathic peptide motif combining long stretches of fluorinated amino acids containing one to fife fluorine substituents in the side chain of ethyl glycine with a short stretch of positively charged lysine residues that mediate solubility in aqueous medium. The structural and biomaterial properties of this new class of compounds will be discussed. This design is comparable to organic co-block polymers. The application of this class of fluoropeptide conjugates for the encapsulation of hydrophobic drugs and their specific delivery to cellular targets will also be shown. In addition, we are investigating how isolated enzymes and whole microorganisms are able to cleave C-F bonds of fluorinated peptides and amino acids. [4] These results open up new avenues for the development of biomaterials containing fluorine.
[1] A.A. Berger, J.-S. Völler, N. Budisa, B. Koksch. Acc. Chem. Res. 2017, 50 (9), 2093
[2] S. Chowdhary, R.F. Schmidt, A.K. Sahoo, T. tom Dieck, T. Hohmann, B. Schade, K. Brademann Jock, A.F. Thünemann, R.R. Netz, M. Gradzielski, B. Koksch. RSC Nanoscale 2022, 14, 10176
[3] T. Hohmann, S. Chowdhary, K. Ataka, J. Er, G. H. Dreyhsig, J. Heberle, B. Koksch. Chem. Eur. J. 2023, e202203860
[4] M. F. Khan, S. Chowdhary, B. Koksch, C. D. Murphy. Environmental Science & Technology 2023, 57, 9762
For upcoming series, please visit the RSC PPSG website.
If you would like to present in future seminars, please contact one of the organisers.
Date: 04-04-2025
Time: 1:00-2:00 pm
Venue: online Zoom seminar
Registration: https://eu01web.zoom.us/meeting/register/u5Ikc-2grT4jH9326Nm6qwWzp1OMYDJlEU9e
Jack Jeffries, University College London
Mining the multitude: Cell free protein expression for metagenomic enzyme discovery
Cell free expression utilises the cellular transcriptional and translational machinery without the other cell processes such as growth and division for protein expression. It has found use in the production of proteins that may be toxic to a host cell, antimicrobial peptides, the screening of genetic parts or for the insertion of non-canonical/ non-natural amino acids. Due to the ability to scale down cell free expression systems and the short time frames needed for generation of quantifiable protein, we are interested in using it to explore the huge sequence space available from Metagenomes to identify candidates for industrial biocatalysis.
Beate Koksch, Freie Universität Berlin
Fluoropeptides as biodegradable biopolymers
Fluorine as a substituent causes drastic changes in the biophysical properties of organic molecules and polymers. This results in highly appreciated properties of drugs and materials that are ubiquitous in our everyday lives today. However, the unique stability of the C-F bond can be problematic if this leads to poor biodegradability. Combining the special material properties of fluoropolymers with the biocompatibility of peptides could be an attractive solution.
The incorporation of fluorine substituents into otherwise hydrophobic amino acid side chains induces a polarity that no other functionality can generate in this form. This special polarity leads to drastic changes in the biophysical properties of peptides in terms of hydrophobicity, lipophilicity, solubility as well as folding and proteolytic stability; criteria that are of utmost importance for biomolecular recognition, self-assembly and, thus, the properties of peptide-based biomaterials. [1] Generally, the combination of fluorine substituents, which lead to the much-described and widely used omniphobic properties in organic polymers, with the water-soluble properties of peptides (depending on their sequence and folding) promises new classes of compounds with extremely interesting properties. Fluoropeptides, which consist exclusively or to a large extent of fluorinated amino acids, offer a wide range of unexplored possibilities in terms of folding, self-assembly and material properties. We have recently taken the first steps into this uncharted scientific territory. [2, 3]
The lecture will present the first polyfluorinated peptides that consist of more than 50% of fluorinated amino acids. They represent an amphipathic peptide motif combining long stretches of fluorinated amino acids containing one to fife fluorine substituents in the side chain of ethyl glycine with a short stretch of positively charged lysine residues that mediate solubility in aqueous medium. The structural and biomaterial properties of this new class of compounds will be discussed. This design is comparable to organic co-block polymers. The application of this class of fluoropeptide conjugates for the encapsulation of hydrophobic drugs and their specific delivery to cellular targets will also be shown. In addition, we are investigating how isolated enzymes and whole microorganisms are able to cleave C-F bonds of fluorinated peptides and amino acids. [4] These results open up new avenues for the development of biomaterials containing fluorine.
[1] A.A. Berger, J.-S. Völler, N. Budisa, B. Koksch. Acc. Chem. Res. 2017, 50 (9), 2093
[2] S. Chowdhary, R.F. Schmidt, A.K. Sahoo, T. tom Dieck, T. Hohmann, B. Schade, K. Brademann Jock, A.F. Thünemann, R.R. Netz, M. Gradzielski, B. Koksch. RSC Nanoscale 2022, 14, 10176
[3] T. Hohmann, S. Chowdhary, K. Ataka, J. Er, G. H. Dreyhsig, J. Heberle, B. Koksch. Chem. Eur. J. 2023, e202203860
[4] M. F. Khan, S. Chowdhary, B. Koksch, C. D. Murphy. Environmental Science & Technology 2023, 57, 9762
For upcoming series, please visit the RSC PPSG website.
If you would like to present in future seminars, please contact one of the organisers.
