Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles

Renthal, Robert; Brancaleon, Lorenzo; Peña, Isaac; Silva, Frances; Chen, L. Y.

doi:10.1016/j.bpc.2011.08.005

Cited by 7 publications

(7 citation statements)

References 41 publications

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“…To investigate the structural changes in the transmembrane part that occur upon transfer from the lipid membrane to SDS micelle environment, a two helix fragment comprising transmembrane helix A and B of bR was recently investigated by FRET [89]. The protein intrinsic tryptophan (helix A) and tyrosine (helix B) residues were utilized.…”

Section: Experimental Approaches To Gain Unique Insight Into Rhodomentioning

confidence: 99%

“…The protein intrinsic tryptophan (helix A) and tyrosine (helix B) residues were utilized. Importantly, the study indicated that disappearance of FRET upon changing the environment does not necessarily indicate structural disruption, but may also be explained by changes in the photophysics of the fluorophores [89]. …”

Section: Experimental Approaches To Gain Unique Insight Into Rhodomentioning

confidence: 99%

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Fluorescence spectroscopy of rhodopsins: Insights and approaches

Alexiev

Farrens

2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Fluorescence spectroscopy has become an established tool at the interface of biology, chemistry and physics because of its exquisite sensitivity and recent technical advancements. However, rhodopsin proteins present the fluorescence spectroscopist with a unique set of challenges and opportunities due to the presence of the light-sensitive retinal chromophore. This review briefly summarizes some approaches that have successfully met these challenges and the novel insights they have yielded about rhodopsin structure and function. We start with a brief overview of fluorescence fundamentals and experimental methodologies, followed by more specific discussions of technical challenges rhodopsin proteins present to fluorescence studies. Finally, we end by discussing some of the unique insights that have been gained specifically about visual rhodopsin and its interactions with affiliate proteins through the use of fluorescence spectroscopy.

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Section: Experimental Approaches To Gain Unique Insight Into Rhodomentioning

confidence: 99%

Section: Experimental Approaches To Gain Unique Insight Into Rhodomentioning

confidence: 99%

Fluorescence spectroscopy of rhodopsins: Insights and approaches

Alexiev

Farrens

2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…Therefore, to understand the peptides conformational changes, inter- or intramolecular interactions, the CD analyses were performed in specific solvents. SDS was used to simulate peptide-membrane interactions, simulating natural biological environments [ 25 ]; TFE induce an α-helix formation and stabilize the secondary structure [ 26 ]; MeOH promotes β-turns conformation The results suggest that all peptides, except peptide 3, tend to adopt β-turns conformation (Fig. 1 ) [ 27 ].…”

Section: Resultsmentioning

confidence: 99%

New linear antiplasmodial peptides related to angiotensin II

Silva

Torres

Silva

et al. 2015

Malar J

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BackgroundAntiplasmodial activities of angiotensin II and its analogues have been extensively investigated in Plasmodium gallinaceum and Plasmodium falciparum parasite species. Due to its vasoconstrictor property angiotensin II cannot be used as an anti-malarial drug.MethodsThis work presents the solid-phase syntheses and liquid chromatography and mass spectrometry characterization of ten linear peptides related to angiotensin II against mature P. gallinaceum sporozoites and erythrocyte invasion by P. falciparum. Conformational analyses were performed by circular dichroism. IC50 assays were performed to identify the ideal concentration used on the biological tests and haemolytical erythrocytic assays were made to verify the viability of the biological experiments. The contractile responses of the analogues were made to evaluate if they are promising candidates to be applied as antiplasmodial drugs.ResultsThe results indicate two short-peptides constituted by hydrophobic residues (5 and 6) with antiplasmodial activity in these models, 89 and 94 % of biological activity against P. gallinaceum sporozoite, respectively, and around 50 % of activity against P. falciparum. Circular dichroism spectra suggested that all the peptides adopted β-turn conformation in different solutions, except peptide 3. Besides the biological assays IC50, the haemolysis assays and contractile response activities were applied for peptides 5 and 6, which did not present expressive results.ConclusionsThe hydrophobic portion and the arginine, tyrosine, proline, and phenylalanine, when present on peptide primary sequence, tend to increase the antiplasmodial activity. This class of peptides can be explored, as anti-malarial drugs, after in vivo model tests.Graphical abstract:The most active peptide presented 94 % activity on P. gallinaceum sporozoites and 53 % inhibited P. falciparum ring forms invasionElectronic supplementary materialThe online version of this article (doi:10.1186/s12936-015-0974-y) contains supplementary material, which is available to authorized users.

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“…In a similar unfolding study, two TM helices of bacteriorhodopsin that are known to associate (helices A and B) were transferred from 1,2‐dioleoylphosphatidylcholine (DOPC) bilayers to SDS micelles . This study involved the use of intrinsic FRET from a tyrosine on one peptide to two tryptophan residues on the other peptide.…”

Section: Fret Studies Of Tm Interactions In Lipid and Detergentmentioning

confidence: 99%

Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET

Khadria

Senes

2015

Biopolymers

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FRET has been widely used as a spectroscopic tool in vitro to study the interactions between transmembrane helices in detergent and lipid environments. This technique has been instrumental to many studies that have greatly contributed to quantitative understanding of the physical principles that govern helix-helix interaction in the membrane. These studies have also improved our understanding of the biological role of oligomerization in membrane proteins. In this review, we focus on the combinations of fluorophores used, the membrane mimetic environments and measurement techniques that have been applied to study model systems as well as biological oligomeric complexes in vitro. We highlight the different formalisms used to calculate FRET efficiency, and the challenges associated with accurate quantification. The goal is to provide the reader with a comparative summary of the relevant literature for planning and designing FRET experiments aimed at measuring transmembrane helix-helix association.

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Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles

Cited by 7 publications

References 41 publications

Fluorescence spectroscopy of rhodopsins: Insights and approaches

Fluorescence spectroscopy of rhodopsins: Insights and approaches

New linear antiplasmodial peptides related to angiotensin II

Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET

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