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. 1994 Sep 19;352(1):87-90.
doi: 10.1016/0014-5793(94)00925-2.

The cyclic structure of the enterococcal peptide antibiotic AS-48

B Samyn  1 , M Martinez-Bueno, B Devreese, M Maqueda, A Gálvez, E Valdivia, J Coyette, J Van Beeumen
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Free article

The cyclic structure of the enterococcal peptide antibiotic AS-48

B Samyn et al. FEBS Lett. .
Free article

Abstract

The complete primary structure of the peptide antibiotic AS-48 produced by Enterococcus faecalis has been determined by chemical degradation analysis. The cyclic nature of this 70 residues containing peptide was demonstrated by plasma desorption mass analysis of the generated peptides and electrospray ionisation mass analysis of the native polypeptide. As far as we know, this is the first example of an antibiotic protein cyclised by a tail-head peptide bond formation and not by branching of the polypeptide side chains.

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