Engineering stable calibration standards for biomedical research
Lead Research Organisation:
University of Oxford
Department Name: Oxford Chemistry
Abstract
Work by Davis has demonstrated the feasibility of new manufacturing routines for sitespecificmodification of proteins. This project aims to establish whether these newmanufacturing processes represent a means of manufacturing precise protein calibrationstandard products offering advantages in terms of product specification, stability, processflexibility, economics and scaling. This will find application in enabling first-in-classquantitative immunoassays and standards for mass spectrometry.
Publications
Boutureira O
(2011)
Direct radiolabelling of proteins at cysteine using [18F]-fluorosugars.
in Chemical communications (Cambridge, England)
Boutureira O
(2012)
Selenenylsulfide-linked homogeneous glycopeptides and glycoproteins: synthesis of human "hepatic Se metabolite A".
in Angewandte Chemie (International ed. in English)
Boutureira Omar
(2012)
Chemical site-selective radiolabelling of proteins using fluorosugars
in ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
Chalker J
(2011)
Methods for converting cysteine to dehydroalanine on peptides and proteins
in Chemical Science
Chalker JM
(2011)
A "tag-and-modify" approach to site-selective protein modification.
in Accounts of chemical research
Chalker JM
(2012)
Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications.
in Angewandte Chemie (International ed. in English)
Chalker Justin M.
(2011)
Reaction engineering for protein modification
in ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
Chalker Justin M.
(2011)
Allyl sulfides enable olefin metathesis in water and on proteins
in ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
Chalker Justin M.
(2011)
Suzuki-Miyaura cross-coupling on protein substrates using a novel palladium-pyrimidine catalyst
in ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
Chang Y-P
(2014)
DISCOVERY OF A SELECTIVE LYSOSOMAL ALPHA-MANNOSIDASE INHIBITOR FROM AN IMINO-SUGAR LIBRARY
in JOURNAL OF PEPTIDE SCIENCE
Description | We worked a chemical method for building proteins that act as 'molecular display units'. By using them to display important peptide motifs, we found a way of getting those peptides to be recognised by antibodies. This, in turn, allowed our commercial partners to improve the calibration of their own antibodies, making their products more precise (and hence valuable). In turn, these 'better' calibrated antibodies are allowing more precise and quantitative use of antibodies as widespread 'reagents' in biological science. |
Exploitation Route | We think that the development of 'better' antibodies will have widespread benefits to improving their use. Beyond that we can envisage using our 'display units' to display all sorts of things in biology, allowing even the design of molecular rulers, for instance. |
Sectors | Chemicals,Pharmaceuticals and Medical Biotechnology |
URL | http://users.ox.ac.uk/~dplb0149/ |
Description | BGD and group members have appeared on the radio, television, (BBD, Channel 5), science festivals around the world (Cheltenham, Kent, Edinburgh, Times Lit., Sydney) describing this work. We have given talks in schools to inspire the next generation. The commercial partners on this work (Badrilla Ltd) have licensed the approach and this increasing their development and growth. |
First Year Of Impact | 2011 |
Sector | Chemicals,Healthcare,Pharmaceuticals and Medical Biotechnology |
Impact Types | Cultural,Societal,Economic |
Company Name | Glycoform Ltd |
Description | drug delivery and glycoprotein specialist; biopharmaceuticals |
Impact | Employed >20 people over 10 years and provided a model for how synthetic protein drugs might be constructed and used. The technology for this company has now been used by major US companies. |
Website | http://isis-innovation.com/news/glycoform-ltd-improve-drug-delivery/ |