Fig. 2: Identification of the TMcin AMP. | Nature Communications

Fig. 2: Identification of the TMcin AMP.

From: Antimicrobial peptide class that forms discrete β-barrel stable pores anchored by transmembrane helices

Fig. 2

a Size-exclusion chromatography of the purified antimicrobial substance on a Superdex 75 column. b Quadrupole mass spectrometry analysis of the purified antimicrobial substance. [M] is the deconvoluted monoisotopic molecular weight (mean ± standard deviation). c N-terminal sequencing result (highlighted), which when combined with the molecular weight identifies the antimicrobial substance as a modified peptide that matches a pre-peptide encoding gene on the BGC (red arrow in Fig. 1b). Arrow denotes the cleavage site of the pre-peptide and the bracket indicates a disulfide bond between two conserved cysteine residues. d Sequence logo of the mature peptide derived from multiple sequence alignment. e AlphaFold2 predicted structure colored by the pLDDT score of the TMcin mature peptide showing a N-terminal TMH and a C-terminal two-stranded β-sheet loop, each end of which is pinned by a disulfide bond (right, magnified). f The molecular lipophilicity potential79 of TMcin-G1905 showing an amphipathic fold (images rotated 120° around the vertical axis). Source data are provided as a Source Data file.

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