I found this paper in which anti-AMPylation monoclonal antibodies are described. Perhaps you can contact the authors.

http://onlinelibrary.wiley.com/doi/10.1002/anie.201103203/abstract

Also, Bellbrook Labs has an anti-AMP antibody that is part of a kit for detection of AMP. Perhaps it could be used to pull down AMPylated peptides.

http://bellbrooklabs.com/products-services/transcreener-hts-assays/amp2-gmp2-assays

Hello Kumar,

From your experience, how does AMP affect the physico-chemical properties of the modified peptides vs their non-modified counterparts? Is there a specific property of the modified peptides that can be used for enrichment?

Hello Gnanesh, hope all's well.

The guys at Basel University Biozentrum have just published this technical brief, "An experimental strategy for the identification of AMPylation targets from complex protein samples" (DOI 10.1002/pmic.201300470; Proteomics 2014, 14, 1048–1052) which may be of great use to you but it is not an enrichment strategy for post-digestion.

Due to the low stoichiometry of AMPylation in peptides, I think you would need a very large amount of starting material. And perhaps using size-exclusion chromatography would be useful as the bulky AMP moiety may separate differently than the unmodified peptide.

Good luck!

Hi Ilian,

 As of now I have no idea whether the addition of AMP increases atleast partly hydrophobicity or hydrophilicity of peptides. If it is figured out could be able to enrich those peptides using respective approaches.

There are reports about enrichment of ADPribosylated peptides using the "standard" phosphopeptide enrichment methods of IMAC and TiO2 e.g. here:

http://www.sciencedirect.com/science/article/pii/S1874391911002909#

AMP being a phosphate moiety less can probably also benefit from those two enrichment strategies.