3rd Annual Academic Symposium - Gana Talapureddy

Protein purification is the fundamental step in individual protein studies. Proteins or peptides can be labeled by affinity tags for easy purification. Biotin is one of the most common tags for protein and nucleic acid purification with neutravidin affinity extraction. To break the extremely strong non-covalent interaction between biotinylated peptides and neutravidin beads, harsh elution like detergent or guanidine treatment are usually used. But the resultant peptides often experienced poor purity. This work optimize the affinity extraction method to purify peptides with neutravidin beads by using biotinylated bovine serum albumin (BSA) tryptic peptides as a model. We developed a new wash step for biotin-neutravidin affinity strategy which leads to pure elution without unbiotinylated peptide contamination.