The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
Author:
Funder
Capes
CNPq
Fapesp
Publisher
Springer Science and Business Media LLC
Subject
Organic Chemistry,Clinical Biochemistry,Biochemistry
Link
https://link.springer.com/content/pdf/10.1007/s00726-021-02982-0.pdf
Reference66 articles.
1. Agadi N, Vasudevan S, Kumar A (2018) Structural insight into the mechanism of action of antimicrobial peptide BMAP-28(1–18) and its analogue mutBMAP18. J Struct Biol 204(3):435–448
2. Alvares DS, Fanani ML, Ruggiero Neto J, Wilke N (2016) The interfacial properties of the peptide Polybia-MP1 and its interaction with DPPC are modulated by lateral electrostatic attractions. Biochim Biophys Acta (BBA) Biomembr 1858(2):393–402
3. Alvares DS, Ruggiero Neto J, Ambroggio EE (2017a) Phosphatidylserine lipids and membrane order precisely regulate the activity of Polybia-MP1 peptide. Biochim Biophys Acta Biomembr 1859(6):1067–1074
4. Alvares DS, Wilke N, Ruggiero Neto J, Fanani ML (2017b) The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state. Chem Phys Lipids 207:38–48
5. Alvares DS, Viegas TG, Ruggiero Neto J (2018a) The effect of pH on the lytic activity of a synthetic mastoparan-like peptide in anionic model membranes. Chem Phys Lipids 216:54–64
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