dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversity of Brasília
dc.date.accessioned2014-05-27T11:28:54Z
dc.date.accessioned2022-10-05T18:47:58Z
dc.date.available2014-05-27T11:28:54Z
dc.date.available2022-10-05T18:47:58Z
dc.date.created2014-05-27T11:28:54Z
dc.date.issued2013-04-09
dc.identifierPLoS ONE, v. 8, n. 4, 2013.
dc.identifier1932-6203
dc.identifierhttp://hdl.handle.net/11449/75091
dc.identifier10.1371/journal.pone.0060818
dc.identifierWOS:000317909600050
dc.identifier2-s2.0-84876038676
dc.identifier2-s2.0-84876038676.pdf
dc.identifier9424346762460416
dc.identifier0000-0002-8059-0826
dc.identifier0000-0002-4767-0904
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3924032
dc.description.abstractAntimicrobial peptides (AMPs) isolated from several organisms have been receiving much attention due to some specific features that allow them to interact with, bind to, and disrupt cell membranes. The aim of this paper was to study the interactions between a membrane mimetic and the cationic AMP Ctx(Ile21)-Ha as well as analogues containing the paramagnetic amino acid 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) incorporated at residue positions n = 0, 2, and 13. Circular dichroism studies showed that the peptides, except for [TOAC13]Ctx(Ile21)-Ha, are unstructured in aqueous solution but acquire different amounts of α-helical secondary structure in the presence of trifluorethanol and lysophosphocholine micelles. Fluorescence experiments indicated that all peptides were able to interact with LPC micelles. In addition, Ctx(Ile21)-Ha and [TOAC13]Ctx(Ile21)-Ha peptides presented similar water accessibility for the Trp residue located near the N-terminal sequence. Electron spin resonance experiments showed two spectral components for [TOAC0]Ctx(Ile21)-Ha, which are most likely due to two membrane-bound peptide conformations. In contrast, TOAC2 and TOAC13 derivatives presented a single spectral component corresponding to a strong immobilization of the probe. Thus, our findings allowed the description of the peptide topology in the membrane mimetic, where the N-terminal region is in dynamic equilibrium between an ordered, membrane-bound conformation and a disordered, mobile conformation; position 2 is most likely situated in the lipid polar head group region, and residue 13 is fully inserted into the hydrophobic core of the membrane. © 2013 Vicente et al.
dc.languageeng
dc.relationPLOS ONE
dc.relation2.766
dc.relation1,164
dc.rightsAcesso aberto
dc.sourceScopus
dc.subject2,2,6,6 tetramethylpiperidine 1 oxyl 4 amino 4 carboxylic acid
dc.subjectcarboxylic acid
dc.subjectceratotoxin like peptide
dc.subjectcyclic AMP
dc.subjectpolypeptide antibiotic agent
dc.subjecttrypsin
dc.subjectunclassified drug
dc.subjectalpha helix
dc.subjectamino terminal sequence
dc.subjectantimicrobial activity
dc.subjectAnura
dc.subjectBacillus subtilis
dc.subjectCandida albicans
dc.subjectcarboxy terminal sequence
dc.subjectcircular dichroism
dc.subjectcontrolled study
dc.subjectCryptococcus neoformans
dc.subjectdrug screening
dc.subjectdrug synthesis
dc.subjectelectron spin resonance
dc.subjectEscherichia coli
dc.subjectfluorescence analysis
dc.subjectfluorescence spectroscopy
dc.subjecthuman
dc.subjecthuman cell
dc.subjecthydrophobicity
dc.subjectHypsiboas albopunctatus
dc.subjectmembrane binding
dc.subjectmicelle
dc.subjectmolecular interaction
dc.subjectnonhuman
dc.subjectprotein secondary structure
dc.subjectPseudomonas aeruginosa
dc.subjectresidue analysis
dc.subjectsequence analysis
dc.subjectspin labeling
dc.subjectStaphylococcus aureus
dc.subjectstructure analysis
dc.titleDynamics and Conformational Studies of TOAC Spin Labeled Analogues of Ctx(Ile21)-Ha Peptide from Hypsiboas albopunctatus
dc.typeArtigo


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