Investigating the ability of antibodies to recognize specific oxidized protein epitopes

Stuart Meredith, Corinne Spickett, Gita Parekh, James Schouten, Helen Griffiths, Paul Davis

Research output: Contribution to journalConference abstractpeer-review


There is a growing awareness that inflammatory diseases have an oxidative pathology, which can result in specific oxidation of amino acids within proteins. Antibody-based techniques for detecting oxidative posttranslational modifications (oxPTMs) are often used to identify the level of protein oxidation. There are many commercially available antibodies but some uncertainty to the potential level of cross reactivity they exhibit; moreover little information regarding the specific target epitopes is available. The aim of this work was to investigate the potential of antibodies to distinguish between select peptides with and without oxPTMs. Two peptides, one containing chlorotyrosine (DY-Cl-EDQQKQLC) and the other an unmodified tyrosine (DYEDQQKQLC) were synthesized and complementary anti-sera were produced in sheep using standard procedures. The anti-sera were tested using a half-sandwich ELISA and
the anti-serum raised against the chloro-tyrosine containing peptide showed increased binding to the chlorinated peptide, whereas the control anti-serum bound similarly to both peptides. This suggested that antibodies can discriminate between similar peptide sequences with and without an oxidative modification. A peptide (STSYGTGC) and its variants with chlorotyrosine or nitrotyrosine were produced. The anti-sera showed substantially less binding to these alternative peptides than to the original peptides the anti-sera were produced against. Work is ongoing to test commercially available antibodies against the synthetic peptides as a comparison to the anti-sera produced in sheep. In conclusion, the antisera were able to distinguish between oxidatively modified and unmodified peptides, and two different sequences around the modification site.
Original languageEnglish
Article numberPP36
Pages (from-to)S31
Number of pages1
JournalFree Radical Biology and Medicine
Issue numberSuppl.1
Early online date28 Aug 2015
Publication statusPublished - Sept 2015
EventSFRR-E/SNFS Meeting Stuttgart 2015 - University of Hohenheim, Stuttgart, Germany
Duration: 1 Sept 2015 → …

Bibliographical note

SFRR-E/SNFS Conference Abstracts, Stuttgart 2015


Dive into the research topics of 'Investigating the ability of antibodies to recognize specific oxidized protein epitopes'. Together they form a unique fingerprint.

Cite this