Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic.


Epidermin is a large peptide antibiotic, which is synthesized in the ribosome via a precursor protein, followed by enzymatic modifications. It was isolated from the culture filtrate of Staphylococcus epidermidis Tü 3298 by adsorption on Amberlite XAD-8. The basic heneicosapeptide amide was chromatographed on Sephadex LH-20 and purified to homogeneity via multiplicative counter-current distributions in one acidic and one neutral system. Tryptic digestion gave the soluble N-terminal fragment epidermin-(1-13)-peptide (P1) and the insoluble C-terminal fragment 2-oxobutyryl-epidermin-(15-21)-peptide amide (P2), each possessing two sulfide ring systems. The heterodetic rings consisted of meso-lanthionine and (2S,3S, 6R)-3-methyllanthionine (P1), meso-lanthionine and C-terminally the new amino acid S-(2-aminovinyl)-D-cysteine (P2). The complex sequence was elucidated via a combination of desulfurization with Raney nickel, enzymatic and acidolytic degradations, gas-phase sequencing, fast-atom bombardment and field-desorption mass spectrometry and NMR spectroscopy.

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@article{Allgaier1986EpiderminSO, title={Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic.}, author={H Allgaier and Guenther Jung and Rolf G{\"{u}nter Werner and Urs Schneider and Hans Z{\"a}hner}, journal={European journal of biochemistry}, year={1986}, volume={160 1}, pages={9-22} }