Phenylalanine interaction with lipid monolayers at different pHs

Cutró, Andrea Carmen; Hollmann, Axel; Cejas, Jimena del Pilar; Maturana, Patricia del Valle; Disalvo, E.A.; Frías, María de los Ángeles

doi:10.1016/j.colsurfb.2015.07.059

Cited by 15 publications

(30 citation statements)

References 26 publications

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“…Follow-up studies demonstrated the ability of amino acid amyloids to bind to lipid membranes (Griffith et al 2014;Cutró et al 2015;R o s ae ta l .2015; Sankaranarayanan 2015), just as observed with protein amyloids (Terzi et al 1997;Jayasinghe and Langen 2007). Therefore, it appears that the phenylalanine amyloids not only share the same morphology and chemical-physical characteristics as protein amyloid but also their specificity toward biological targets.…”

Section: Nonproteinaceous Amyloidsmentioning

confidence: 90%

Metabolite amyloids: a new paradigm for inborn error of metabolism disorders

Gazit

2016

J of Inher Metab Disea

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The formation of ordered amyloid assemblies is associated with major human degenerative disorders, including Alzheimer's disease, Parkinson's disease, and type 2 diabetes. Amyloid fibrils are elongated nanoscale structures that bind to specific dyes (including thioflavin T and Congo red). Amyloid fibrillar assemblies or their early intermediates are known to induce apoptotic cytotoxic effect. Until recently, amyloid fiber formation was observed only with proteins and peptides. We reported in 2012 that a single amino acid, phenylalanine, could also form typical amyloid fibrils with the same morphology, dye-binding specificity, and electron diffraction pattern as protein amyloids. X-ray crystallography demonstrated the formation of supramolecular β-sheet-like organization by phenylalanine at its zwitterionic form. Metabolite amyloids had pronounced cytotoxicity that could be depleted by treatment with antibodies raised against the phenylalanine structures. We suggested that the observed amyloid formation could explain some of the symptoms observed in phenylketonuria (PKU) upon the accumulation of phenylalanine. Follow-up studies by other groups revealed the ability of phenylalanine amyloids to bind to membranes, as observed with protein amyloids. Furthermore, the doxycycline amyloid formation inhibitor was shown to also affect the formation of phenylalanine amyloids. In 2015, it was reported that other metabolites involved in metabolic disorders, including adenine, uracil, tyrosine, and orotic acid, could form amyloid-like assemblies. It was further demonstrated that the assemblies induce apoptotic cell death. Taken together, we suggest a new hypothesis to understand the etiology of degenerative processes observed in inborn error of metabolism disorders and indicate new avenues for treatment.

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Section: Nonproteinaceous Amyloidsmentioning

confidence: 90%

Metabolite amyloids: a new paradigm for inborn error of metabolism disorders

Gazit

2016

J of Inher Metab Disea

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“…On the other hand, when Phe is added to condensed DPPC, the area decreases below 4 to 5 mM Phe and increases significantly above 5 mM (Figure 3, red symbols). The slight area decrease may be due to Phe insertion in vacancies (packing defects) present in the LC phase 11 that may reduce the repulsion between head groups producing a local contraction. When those vacancies are occupied, above 5 mM Phe appears to induce an area increase.…”

Section: Resultsmentioning

confidence: 99%

Effects of Phenylalanine on the Liquid-Expanded and Liquid-Condensed States of Phosphatidylcholine Monolayers

2019

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Background:Phenylalanine (Phe) is involved in physiological and pathological processes in cell membranes in which expanded and condensed states coexist. In this direction, it was reported that surface hydration is important for the binding affinity of the amino acid which significantly perturbs 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) monolayer structure and morphology. A deeper insight showed that Phe inserts in DPPC monolayer defects as a monomer at pH 5 and forms aggregates that adsorb to the membrane surface generating a reconfiguration of the lipid arrangement in areas of higher packing. This new arrangement in the monolayer causes the reorientation of dipoles of lipid and water molecules which is congruent with the dehydration and surface tension changes reported above. With this background, this article studies the affinity of Phe in liquid-expanded 1,2-dimyristoyl-sn-glycero-3 phosphocholine (LE DMPC) and liquid-condensed 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (LC DPPC) monolayers and their effects on membrane properties.Results:The adsorption of Phe can be described by a cooperative process in non-independent sites suggesting that Phe/lipid systems reorganize to form new structures at a high degree of coverage. Compressibility modulus and Brewster angle microscopy (BAM) images allow to propose that Phe causes a new phase in 1,2-dimyristoyl-sn-glycero-3 phosphocholine (DMPC) and DPPC.Conclusions:Phe imposes new arrangements in the lipid phase to form new structures with different compressibility behavior than lipid binary mixtures of DMPC and DPPC. Phe interaction with the LC and LE phases gives place to a process in which a synergistic effect between non-independent sites can be produced. These features of Phe/lipid interaction would be of great importance to understand the multiple effects of Phe on cell membranes.

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“…The presence of defects in the membrane packing determines the binding and stabilization of peptides containing Arg and Phe motifs [67][68][69] The disruption of the water network around the phenyl group and the membrane defect has been invoked to explain the negative free energy of the formation a PC-Phe (phosphocholine-phenylalanine) complex in the presence of water. An important observation was that a dipole potential decrease was produced in this interaction which was explained by the orientation of the carboxylate opposing to the CO of the lipids [66,70]. As described in Figure 9, carbonyl groups are one of the hydration centers in which interfacial water is distributed.…”

Section: Topological Effects Of Osmotic Shrinkage Defects In Packingmentioning

confidence: 97%

The Role of Water in the Responsive Properties in Lipid Interphase of Biomimetic Systems

Disalvo¹,

Frías²

2019

Liposomes - Advances and Perspectives

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The lack of details in the hydration properties of lipid bilayers hinders the design of biomimetic systems that, as liposomes and vesicles, may be used for biotechnological and medical purposes. In this chapter, studies indicate water as a membrane dynamic component determining the affinity and response of lipid membranes to amino acids, peptides and others stimuli. Based on thermodynamic analysis in lipid monolayers and its comparison with swelling shrinkage processes in liposomes and vesicles, it is concluded that: (1) the interphase of a lipid bilayer in a bidimensional solution of hydrated polar groups imbibed in labile water can be exchanged with the media by osmosis and or expansion-compression. (2) Excess water beyond the hydration shell (confined water) has solvent properties for additives in the bulk water phase and confers free energy that is in excess for binding of amino acids and peptides.(3) Dissolution in the water membrane phase changes the water activity (a w ) and affects the surface pressure. (4) Defects may be formed by the compression of bilayers in which carbonyl groups organized water differently. These studies indicate that a deeper understanding of the role of lipid bilayers in cellular biology and support the development of future lipid-based biotechnology that should necessarily include the role of water as a membrane dynamic component.

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Phenylalanine interaction with lipid monolayers at different pHs

Cited by 15 publications

References 26 publications

Metabolite amyloids: a new paradigm for inborn error of metabolism disorders

Metabolite amyloids: a new paradigm for inborn error of metabolism disorders

Effects of Phenylalanine on the Liquid-Expanded and Liquid-Condensed States of Phosphatidylcholine Monolayers

The Role of Water in the Responsive Properties in Lipid Interphase of Biomimetic Systems

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