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. Author manuscript; available in PMC: 2011 Nov 1.
Published in final edited form as: Peptides. 2010 Aug 14;31(11):1957–1965. doi: 10.1016/j.peptides.2010.08.008

Figure 5.

Figure 5

A. Tricine-SDS-PAGE of the purification steps used to achieve pure HHC-10 from a 1 L shaking flask expression, fraction 12 in lane 2 corresponds to the sample used for mass determination. Again, no larger protein contaminants could be found, indicating that the higher bands visible in the gel are possibly aggregates of HHC-10, which could be avoided in a different solvent.

B. MALDI profile for HHC-10 showing the correct mass of 1444 Da.

C. Direct comparison of MIC for both synthetic and recombinant HHC-10 using E. coli K12 and P. aeruginosa PA014. The recombinant HHC10 showed a slightly higher MIC for E. coli and P. aeruginosa.