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Identifying structurally stable peptides

A new method for diagnostics and therapeutics development

A new method of identifying peptides that retain the structural, conformational and/or antigenic properties of a particular region of a full protein.


  • Peptides for medicine/therapy, for diagnostic and prognostic/test assays and procedures, and as vaccine candidates

Development Status

  • Undergoing validation

IP Status

  • Priority patent application filed 2021

Commercial Offerings

  • Technology available for licensing and/or co-development


Protein structure and conformation play a key role in the generation of an immune response and it is therefore critical to identify the relevant “hot spots” within the protein that trigger the body’s immune defence. Existing methods and tools attempt the identification of immunogenic regions within proteins, without specific understanding of the potential peptide stability and/or conformation.

An innovative approach has been developed for the rapid identification of stable peptides that retain the structural, conformational and/or antigenic properties of a particular region of a full protein. The technique can be used to derive short, immunogenic peptides that have considerable use in diagnostic and prognostic methods, antibody detection and profiling (‘fingerprinting’), vaccine development and/or monitoring of vaccine performance, and accurate variant detection and measurement.


A new computational method based on rigorous thermodynamic predictions allows the identification and prediction of peptide sequences that retain the structural stability and conformational features which characterise that region of the full protein. Peptide sequences derived in this way are likely to be good candidates for immunogenic sites and the production of antibodies. Proof-of-concept experiments were carried out within the context of SARS-CoV-2 to validate the identification of peptides and their application in developing a next-generation SARS-CoV-2 serology tests.

The method was used to identify short SARS-CoV-2 S-protein derived peptide sequences and to demonstrate that a combination of 5 peptides could detect antibody responses to infection by SARS-Cov-2 virus with 100% sensitivity and 95% specificity. These peptides are shorter than those used in commercial serology tests and allow to discriminate variants, assess whether the immunity is vaccine-induced or is the result of previous exposure to the infection, and assess vaccine effectiveness.

The patented technology requires few peptides to be tested and therefore facilitates the rapid selection of immunogenic peptide.


  • Rapid selection of immunogenic peptides based on rigorous thermodynamic predictions
  • Use of short peptide sequences with better signal-to-noise ratio
  • Peptides that have protein modifications (e.g. N-glycosylation) can be further prioritised
  • High specificity and sensitivity – in the context of SARS-Cov-2 virus serology test, with 100% sensitivity and 95% specificity
  • Discrimination between variants
  • Distinguish antibody response to vaccination from antibody response to viral infection
  • Correlation with clinical outcomes
  • Antibody fingerprinting


Manuscript in preparation.

Please note, the header image is purely illustrative. Source: Fusion Medical Animation via Unsplash.

Quote: TEC1104372

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Dr Mokdad Mezna

Technology Transfer Manager
The Institute of Genetics and Cancer
The Usher Institute