Avacta Group Plc (LON:AVCT) has told investors that Affimer reagents continue to excite the scientific community, with a record nine research papers on the subject already penned in 2017.
That compares with just two written last year, so interest in the area is clearly growing.
READ: Pioneering Avacta making progress on all fronts
Two papers from the “world-renowned laboratory” of David Komander at the University of Cambridge have been published recently in two “important” international journals.
The articles describe the use of Affimers that recognise important cell signals called the “diubiquitin linkages”, which are thought to be involved in many diseases.
A paper in the eLife journal from a group at the University of Leeds which “showcases the key benefits” of the technology proved so popular that it is ranked in the top 5% of all the 8.4mln papers ever tracked by Altmetric.
Interest a validation of Affimer technology
“Independent scientific reports featuring Affimer reagents are strong validations of the technology and highly influential indirect marketing,” said chief executive Alastair Smith.
“During 2017, nine Affimer scientific papers have been published, compared with two in 2016 and four in 2015, and are being read by an ever widening audience; a strong indication of the growing awareness and adoption of the Affimer technology.
“As well as being a bumper year for Affimer publications, it is particularly pleasing to see reports of Affimers' key benefits in the most prestigious scientific journals and I look forward to seeing this trend continue in 2018.”
What are affimers?
Affimers are small, engineered proteins, some of which are of human origin and some of them plant-derived. They are capable of binding specific molecular targets, in a similar way to antibodies.
However, compared with antibodies, Affimers have several innovative and distinctive features, which could potentially make them a better tool for several diagnostic and therapeutic applications.
They are smaller, quicker to manufacture and easier to format, but they maintain antibody-like biologic activity when binding a target.