title: A novel method for the N-terminal modification of native proteins.
abstract: The formation of structurally defined bioconjugates of proteins hinges on their regioselective modification. Toward this goal a novel method is described here using the commercial IgA protease to attach a nonnatural peptidic moiety to the N-terminus of predisposed proteins by means of a kinetically controlled reverse proteolysis in water. The process requires an H-Ala-Pro N-terminal sequence and then furnishes a selectively modified conjugate under nondenaturing and nondestructive conditions in acceptable yield. The method lends itself to the N-terminal introduction of orthogonal moieties that may be elaborated further.
authors.affiliation: Institut für Organische Chemie und Biochemie, Technische Universität München, 85747 Garching, Germany.
authors.forename: Marzena
authors.initials: M
authors.lastname: Lewinska
authors.forename: Christian
authors.initials: C
authors.lastname: Seitz
authors.forename: Arne
authors.initials: A
authors.lastname: Skerra
authors.forename: Franz P
authors.initials: FP
authors.lastname: Schmidtchen
mesh_terms: D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000032:analysis / Q000138:chemical synthesis* / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D010446:Peptide Fragments; D011506:Proteins; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase