Design and synthesis of amphipathic antimicrobial peptides.

摘要: A large proportion of antimicrobial peptides share a common structural feature that is critical to their activity, i.e. amphipathic alpha-helices. The amphipathy polypeptide chain can be quantitated through the value hydrophobic moment. Generally, are characterized by high moment and low hydrophobicity values. Using these criteria we have identified two short segments possess properties associated with known peptides. in vitro assays segment derived from protein perforin displays no antifungal or antibacterial activity and, while showing alpha-helicity buffer liposomes, exhibits modest degree alpha-helical structure presence inducer, 2,2,2-trifluoroethanol. However, rational modifications result derivative which assumes an conformation potent against plant fungal pathogens, has significant effects leakage fluorescent dye acidic liposomes devoid hemolytic activity. Results also presented for human immunodeficiency virus envelope protein. We suggest identification putative structures proteins may provide useful starting strategy design synthesis