Sequence analysis of lantibiotics: chemical derivatization procedures allow a fast access to complete Edman degradation.
Lantibiotics are antibiotic peptides produced via ribosomal synthesis of precursor proteins by gram-positive bacteria. They contain various unusual post-translational modifications, which include the formation of sulfide rings by lanthionine or beta-methyllanthionine, and 2,3-didehydroamino acids. The N-terminus may be blocked by a 2-oxobutyryl group and the C-terminus may be inaccessible in some of the lantibiotics. Due to these modifications the analysis of such peptides is very tedious. Chemical modifications using an ethanethiol-containing reaction mixture and/or trifluoroperacetic acid treatment were used to solve these analytical problems. Investigating the tetracyclic 22-peptide gallidermin and the N-terminally blocked tricyclic 34-peptide Pep5 as examples, a novel access to the primary structure of lantibiotics is demonstrated.
Meyer
H E
HE
Abteilung Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Germany.
Heber
M
M
Eisermann
B
B
Korte
H
H
Metzger
J W
JW
Jung
G
G
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000378:metabolism; D001430:Bacteriocins; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D013058:Mass Spectrometry / Q000379:methods; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D010455:Peptides; D011145:Polyvinyls; D011499:Protein Processing, Post-Translational; D017421:Sequence Analysis / Q000379:methods*; D005465:Fluorocarbon Polymers
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D008567:Membranes, Artificial; D010455:Peptides; D011145:Polyvinyls; C057656:gallidermin; C024865:polyvinylidene fluoride; D005465:Fluorocarbon Polymers; C054222:lantibiotic Pep5