The development of peptide-based metal-binding tags is highly desirable because the tag can be incorporated inline with the protein and used in a large number of applications, including imaging and therapy.  Our lab discovered a novel tripeptide known as the metal abstraction peptide (MAP), which has advantageous chemical properties for use as a tag in such applications.  Several model proteins were selected and tagged in various positions to assess the stability of the tagged protein and the MAP tag in the context of protein systems.  The MAP tag was genetically engineered into the plasmid and expressed in E. coli to generate the MAP-tagged variants.  As a control for interpreting observed differences in protein stability, native protein was analyzed alongside metal-bound MAP-tagged protein.  Various analytical methods were used to confirm metal incorporation and to characterize MAP tag and protein stability.  MAP-tagged variants were prepared using different solution conditions to investigate extrinsic effects on conjugate stability.

Assessing the stability of MAP-tagged protein conjugates

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.