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Updated: Feb 8, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
Effect of Acylation on the Antimicrobial Activity of Temporin B Analogues
Concetta Avitabile1, Luca Domenico D'Andrea1, Elisabetta D'Aversa2
1Institute of Biostructure and Bioimaging, National Research Council-CNR, via Mezzocannone 16, 80134, Naples, Italy.
Abstract:
New peptides derived from the natural antimicrobial temporin B were obtained. The design, antimicrobial activity, and characterization of the secondary structure of peptides in the presence of bacterial cells is described herein. TB_KKG6K (KKLLPIVKNLLKSLL) has been identified as the most active analogue against Gram-positive and -negative bacteria, compared with natural temporin B (LLPIVGNLLKSLL) and TB_KKG6A (KKLLPIVANLLKSLL). Acylation with hydrophobic moieties generally led to reduced activity; however, acylation at the 6-position of TB_KKG6K led to retained sub-micromolar activity against Staphylococcus epidermidis.
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