Cell Selectivity of an Antimicrobial Peptide Melittin Diastereomer with D-amino Acid in the Leucine Zipper Sequence
2007
Zhu, Wan Long (Chosun University, Gwangju, Republic of Korea) | Nan, Yong Hai (Chosun University, Gwangju, Republic of Korea) | Hahm, K.S. (Chosun University, Gwangju, Republic of Korea) | Shin, S.Y. (Chosun University, Gwangju, Republic of Korea), E-mail: syshin@chosun.ac.kr
Melittin (ME), a linear 26-residue non-cell-selective antimicrobial peptide, displays strong lytic activity against bacterial and human red blood cells. To design ME analogue with improved cell selectivity, we synthesized a melittin diastereomer (ME-D) with D-amino acid in the leucine zipper sequence (Leu-6, Lue-13 and Ile-20). Compared to ME, ME-D exhibited the same or 2-fold higher antibacterial activity but 8-fold less hemolytic activity. Circular dichroism analysis revealed that ME-D has much less α-helical content in α-helical content in the presence of zwitterionic EYPC/cholesterol (10 : 1, w/w) liposomes compared to negatively charged EYPE/EYPG (7 : 3, w/w) liposomes.
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