Next Article in Journal
An Investigation of the Effects of Self-Assembled Monolayers on Protein Crystallisation
Next Article in Special Issue
Dietary Polyunsaturated Fatty Acids and Inflammation: The Role of Phospholipid Biosynthesis
Previous Article in Journal
Enhanced Inhibition of Bladder Cancer Cell Growth by Simultaneous Knockdown of Antiapoptotic Bcl-xL and Survivin in Combination with Chemotherapy
Previous Article in Special Issue
Phospholipids at the Interface: Current Trends and Challenges
Open AccessArticle

Contribution of the Tyr-1 in Plantaricin149a to Disrupt Phospholipid Model Membranes

Institute of Physics of Sao Carlos, University of Sao Paulo, Av. Trabalhador Saocarlense 400, Sao Carlos, SP 13560-970, Brazil
Institute of Advanced Chemistry of Catalonia (IQAC-CSIC), Barcelona 08034, Spain
Department of Organic Chemistry, National University of the Litoral, Santa Fe C.C.242 (3000), Argentina
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2013, 14(6), 12313-12328;
Received: 21 December 2012 / Revised: 7 May 2013 / Accepted: 25 May 2013 / Published: 7 June 2013
(This article belongs to the Special Issue Phospholipids: Molecular Sciences 2012)
Plantaricin149a (Pln149a) is a cationic antimicrobial peptide, which was suggested to cause membrane destabilization via the carpet mechanism. The mode of action proposed to this antimicrobial peptide describes the induction of an amphipathic α-helix from Ala7 to Lys20, while the N-terminus residues remain in a coil conformation after binding. To better investigate this assumption, the purpose of this study was to determine the contributions of the Tyr1 in Pln149a in the binding to model membranes to promote its destabilization. The Tyr to Ser substitution increased the dissociation constant (KD) of the antimicrobial peptide from the liposomes (approximately three-fold higher), and decreased the enthalpy of binding to anionic vesicles from −17.2 kcal/mol to −10.2 kcal/mol. The peptide adsorption/incorporation into the negatively charged lipid vesicles was less effective with the Tyr1 substitution and peptide Pln149a perturbed the liposome integrity more than the analog, Pln149S. Taken together, the peptide-lipid interactions that govern the Pln149a antimicrobial activity are found not only in the amphipathic helix, but also in the N-terminus residues, which take part in enthalpic contributions due to the allocation at a lipid-aqueous interface. View Full-Text
Keywords: antimicrobial peptide; membrane models; peptide-lipid interaction; plantaricin antimicrobial peptide; membrane models; peptide-lipid interaction; plantaricin
MDPI and ACS Style

Lopes, J.L.S.; Gómara, M.J.; Haro, I.; Tonarelli, G.; Beltramini, L.M. Contribution of the Tyr-1 in Plantaricin149a to Disrupt Phospholipid Model Membranes. Int. J. Mol. Sci. 2013, 14, 12313-12328.

Show more citation formats Show less citations formats

Article Access Map by Country/Region

Only visits after 24 November 2015 are recorded.
Search more from Scilit
Back to TopTop