Volume 17, Issue 10, Pages (October 2010)

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Volume 17, Issue 10, Pages 1151-1160 (October 2010) Effect of Bioengineering Lacticin 3147 Lanthionine Bridges on Specific Activity and Resistance to Heat and Proteases Srinivas Suda, Alja Westerbeek, Paula M. O'Connor, R. Paul Ross, Colin Hill, Paul D. Cotter Chemistry & Biology Volume 17, Issue 10, Pages 1151-1160 (October 2010) DOI: 10.1016/j.chembiol.2010.08.011 Copyright © 2010 Elsevier Ltd Terms and Conditions

Figure 1 Structures of the Lacticin 3147 Peptides Ltnα and Ltnβ Lan (Ala-S-Ala) and meLan (Abu-S-Ala) bridges are indicated. See also Figure S1. Chemistry & Biology 2010 17, 1151-1160DOI: (10.1016/j.chembiol.2010.08.011) Copyright © 2010 Elsevier Ltd Terms and Conditions

Figure 2 Ring A Mutants of Ltnα Mass of the bioengineered peptides, predicted structures, and visual demonstration of antimicrobial activity of 50 μl bioengineered peptide when combined with wild-type sister peptide (both at 2.5 μM concentrations) against L. lactis HP and broth-based MIC determination of antimicrobial activity against L. lactis HP and M. luteus. a, mass difference following cyanylation is in brackets; ∗, D-chiral center. Chemistry & Biology 2010 17, 1151-1160DOI: (10.1016/j.chembiol.2010.08.011) Copyright © 2010 Elsevier Ltd Terms and Conditions

Figure 3 Lan-meLan Interconversion of Rings B–F Mass of the bioengineered peptides, predicted structures, and visual demonstration of antimicrobial activity of 50 μl bioengineered peptide when combined with wild-type sister peptide (both at 2.5 μM concentrations) against L. lactis HP and broth-based MIC determination of antimicrobial activity alone or with equimolar concentrations of complementary sister peptide against L. lactis HP and M. luteus. ∗, wild-type sister peptide used unless stated otherwise. Chemistry & Biology 2010 17, 1151-1160DOI: (10.1016/j.chembiol.2010.08.011) Copyright © 2010 Elsevier Ltd Terms and Conditions