A novel method for the N-terminal modification of native proteins.
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.
Lewinska
Marzena
M
Institut für Organische Chemie und Biochemie, Technische Universität München, 85747 Garching, Germany.
Seitz
Christian
C
Skerra
Arne
A
Schmidtchen
Franz P
FP
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
D010446:Peptide Fragments; D011506:Proteins; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase