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.
Effect of Acylation on the Antimicrobial Activity of Temporin B Analogues
Avitabile C;D'Andrea LD;
2018
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.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
