The structure of polymyxin T1. Studies on antibiotics from the genus Bacillus. XXII.

Abstract

Amino acid analysis of the acid hydrolyzate of polymyxin T1 [an antibacterial antibiotic] revealed the amino acid composition. Isolation of the constituent amino acids and measurement of their optical activities clarified their chiralites. These were 2,4-diaminobutyric acid (6L), Thr(1L), Leu(2L) and Phe(1D). The constituent fatty acid was identified as anteisononanoic acid by gas chromatography and mass spectrometry. Deacylation with polymyxin acylase afforded deacyl polymyxin T. Successive Edman degradation on deacyl polymyxin T revealed most of its amino acid sequence. The chemical cleavage reaction for fragmentation of threonyl peptide on penta(DNP)-polymyxin T1 cleaved it at the C-terminal side of the Thr residue to afford a DNP-octapeptide, whose sequence was clarifed by Edman degradation. Thus, the structure of polymyxin T1 was determined.