Theia Metals

Technology

About our Technology

Next-Generation Technology Platform

To address the mining industry’s challenge of “making more metals with less”, Theia MetalsTM has developed a multi-disciplinary platform that unites proven technologies with proprietary innovations. The goal: to produce large volumes of target-specific peptides at industrial-scale cost.

Core Components

The Theia Metals' platform integrates four core components:

Phage Display: The Engine Behind Peptide Selection

Phage display, developed in 1985 by George Smith, uses bacteriophages (viruses that infect bacteria) to express billions of peptide sequences on their surface. When exposed to a specific mineral or metal target, only the strongest binding phages are retained, amplified, and selected over multiple rounds. The DNA of these binding phages reveals the exact peptide structure for synthesis or further development.

This technique has been widely used across industries - resulting in commercial peptides for biotech, pharmaceuticals, food, cosmetics, agriculture, and biosensing. It’s proven that peptides can be made to bind virtually any surface, including metals and minerals.

Peptide Selection Using Phage Display - A large library of diverse peptides are generated on the surface of bacteriophage using a now classical process of Phage Display.

Schematic Representation of Phage Display - Cloning foreign DNA into the gene which encodes one of the phage coat proteins leads to the expression of the guest amino acid sequence as part of the relevant coat protein on the phage surface. In phage display the displayed peptide (phenotype: tested for binding to target) and its encoding nucleotide sequence (genotype) are physically linked together in an individual phage particle. When the inserted foreign DNA is a large library of different DNA sequences (one sequence incorporated for each phage particle), the expressed peptides corresponding to the DNA diversity are correspondingly diverse in amino acid sequence. The diverse peptide sequences at the end of the phage particle are then tested for their ability to bind the phage (and their DNA) to the target metal or mineral. Bound phage are recovered after washing non-bound phage away, amplified in bacteria and retested in sequential rounds of “panning” to identify binding phage and the corresponding peptide sequence. (diagram from J. biomedical Science 23: article 66, 2016)
Schematic Representation of Phage Display - Cloning foreign DNA into the gene which encodes one of the phage coat proteins leads to the expression of the guest amino acid sequence as part of the relevant coat protein on the phage surface. In phage display the displayed peptide (phenotype: tested for binding to target) and its encoding nucleotide sequence (genotype) are physically linked together in an individual phage particle. When the inserted foreign DNA is a large library of different DNA sequences (one sequence incorporated for each phage particle), the expressed peptides corresponding to the DNA diversity are correspondingly diverse in amino acid sequence. The diverse peptide sequences at the end of the phage particle are then tested for their ability to bind the phage (and their DNA) to the target metal or mineral. Bound phage are recovered after washing non-bound phage away, amplified in bacteria and retested in sequential rounds of “panning” to identify binding phage and the corresponding peptide sequence. (diagram from J. biomedical Science 23: article 66, 2016)

As shown above, each bacteriophage bears a particular short peptide sequence encoded by DNA inside the phage particle. The population of phage bearing a diverse library of peptide structures is then “panned” in sequential rounds for their ability to bind to the immobilised target metal or mineral (diagram below)

Biopanning for Identification of Target-Specific Phage-Displayed Peptides - Incubation of a randomised peptide phage display library with the mineral or metal target is followed sequentially by multiple washing steps (to remove unbound phage), recovery of target-bound phage, and their amplification through bacterial infection. These steps are repeated 3–5 rounds. Finally, selected phage clones displaying peptides with the highest affinity towards the target are identified through DNA sequencing. (diagram from J. biomedical Science 23: article 66, 2016) .
Biopanning for Identification of Target-Specific Phage-Displayed Peptides - Incubation of a randomised peptide phage display library with the mineral or metal target is followed sequentially by multiple washing steps (to remove unbound phage), recovery of target-bound phage, and their amplification through bacterial infection. These steps are repeated 3–5 rounds. Finally, selected phage clones displaying peptides with the highest affinity towards the target are identified through DNA sequencing. (diagram from J. biomedical Science 23: article 66, 2016) .

Peptides in Mining: Untapped Until Now

Since the first metal-binding peptide discovery in 1997, and further work in 2008–2018 identifying peptides for chalcopyrite and sphalerite, hundreds of mineral-specific peptides have been documented in academic literature. However, no peptide-based beneficiation process has reached pilot or commercial scale, primarily due to the high cost and limited scalability of solid-phase peptide synthesis.

Phage particles themselves are not suitable for industrial use, and until recently, peptide production at mining scale (kg - tonne quantities) was economically unfeasible.

Theia Metals' Breakthrough

Theia Metals bridges this gap by leveraging:

  • Recent breakthroughs in recombinant peptide production - dramatically lowering cost at scale

  • Innovative particle-peptide presentation formats - making separation and reuse practical

Through these advances, Theia Metals enables mining to finally benefit from the molecular specificity, diversity, and environmentally friendly nature of peptides - transforming the way minerals and metals are separated.