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Synthesis and Conformational Analysis by CD Spectroscopy of Lantibiotic Leader, Pro- and Pre-Peptides

✍ Scribed by Beck-Sickinger, Annette G. ;Jung, Günther

Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
646 KB
Volume
1993
Category
Article
ISSN
0947-3440

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✦ Synopsis

Abstract

In order to investigate the conformational properties of the precursor proteins of lanthionine‐containing bacteriocins we synthesized the leader peptides of the pre‐lantibiotics of gallidermin, epidermin, Pep5, nisin, subtilin, the C‐terminal 30‐mer segment of pre‐cinnamycin, propeptide segments of Pep5 and gallidermin and the complete pre‐gallidermin, which consists of 52 residues. The peptides were synthesized in a step‐by‐step synthesis by the Fmoc/__t__Bu strategy using an optimized procedure for the synthesis of large peptides. All peptides were analyzed by HPLC and characterized by electrospray mass spectrometry and amino acid analysis. Circular dichroism spectra exhibited strong α‐helical Cotton effects even at a low concentration of trifluoroethanol for all N‐terminal leader peptides. Comparative investigations of the C‐terminal propeptide segments led to a model of the conformation of the prepeptides of Pep5 and gallidermin in aqueous and lipophilic environments. In addition, circular dichroism investigations on the synthetic precursor protein of gallidermin and the isolated natural pre‐Pep5 were performed.

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## SYNOPSIS 0-Endorphin has been studied in SDS micelles by one-and two-dimensional nmr spectroscopy ( 1D and 2D nmr) , and to explore the influence of peptide length and composition on the polypeptide structure, the investigation was extended to a number of fragments. The nmr results are compare