The effect of acidic residues and amphipathicity on the lytic activities of mastoparan peptides studied by fluorescence and CD spectroscopy |
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Authors: | Natália Bueno Leite Laiana Cristina da Costa Dayane dos Santos Alvares Marcia Perez dos Santos Cabrera Bibiana Monson de Souza Mário Sérgio Palma João Ruggiero Neto |
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Institution: | 1.Department of Physics IBILCE,S?o Paulo State University,S?o José do Rio Preto,Brazil;2.Center of Studies of Social Insects, Department of Biology-IB,S?o Paulo State University,S?o José do Rio Preto,Brazil |
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Abstract: | Some mastoparan peptides extracted from social wasps display antimicrobial activity and some are hemolytic and cytotoxic.
Although the cell specificity of these peptides is complex and poorly understood, it is believed that their net charges and
their hydrophobicity contribute to modulate their biological activities. We report a study, using fluorescence and circular
dichroism spectroscopies, evaluating the influence of these two parameters on the lytic activities of five mastoparans in
zwitterionic and anionic phospholipid vesicles. Four of these peptides, extracted from the venom of the social wasp Polybia paulista, present both acidic and basic residues with net charges ranging from +1 to +3 which were compared to Mastoparan-X with three
basic residues and net charge +4. Previous studies revealed that these peptides have moderate-to-strong antibacterial activity
against Gram-positive and Gram-negative microorganisms and some of them are hemolytic. Their affinity and lytic activity in
zwitterionic vesicles decrease with the net electrical charges and the dose response curves are more cooperative for the less
charged peptides. Higher charged peptides display higher affinity and lytic activity in anionic vesicles. The present study
shows that the acidic residues play an important role in modulating the peptides’ lytic and biological activities and influence
differently when the peptide is hydrophobic or when the acidic residue is in a hydrophilic peptide. |
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