2011
DOI: 10.1111/j.1471-4159.2010.07000.x
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Abstract: J. Neurochem. (2011) 116, 696–701. Abstract Acidic lipids are known to both catalyze amyloid fiber formation by amyloidogenic peptides/proteins and induce formation of ‘amyloid‐like’ fibrils by non‐amyloidogenic proteins. In this work, we describe the application of state‐of‐the‐art time‐resolved Förster resonance energy transfer methodologies to the characterization of the supramolecular structure of the aggregates formed by both a cationic peptide (hexalysyltryptophan) and a basic non‐amyloidogenic protein (… Show more

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Cited by 8 publications
(5 citation statements)
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“…Additionally, an interfacial aggregation phenomenon would be consistent with the long-time-scale saturation effects observed in Phe surface adsorption experiments (i.e., the nondiffusive process mentioned earlier), although it is possible that this long-time-scale saturation is due to another slow process, such as intercalation into the membrane or a change in ionization state. Interestingly, phospholipid–water interfaces have been shown to promote aggregation of a variety of peptide sequences ,, through increased local concentration and two-dimensional diffusion when the peptides are bound to phospholipid membranes . One specific example is the toxic misfolding of human islet amyloid polypeptide (hIAPP) .…”
Section: Resultsmentioning
confidence: 99%
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“…Additionally, an interfacial aggregation phenomenon would be consistent with the long-time-scale saturation effects observed in Phe surface adsorption experiments (i.e., the nondiffusive process mentioned earlier), although it is possible that this long-time-scale saturation is due to another slow process, such as intercalation into the membrane or a change in ionization state. Interestingly, phospholipid–water interfaces have been shown to promote aggregation of a variety of peptide sequences ,, through increased local concentration and two-dimensional diffusion when the peptides are bound to phospholipid membranes . One specific example is the toxic misfolding of human islet amyloid polypeptide (hIAPP) .…”
Section: Resultsmentioning
confidence: 99%
“…9,10 On the other hand, the process of polypeptide fibrillization was shown to be modulated by lipid−peptide interactions and to be able to disturb membrane function. 11, 12 Despite the vast knowledge currently being amassed on the many functions of aromatic residues and even single aromatic amino acids, it is still quite difficult to obtain molecular-level information on the causes and mechanisms of these functions. To aid in the molecular-level description of interactions involving biological lipid membranes, the simplified model system of a monolayer at the air−water interface is often used rather than the bilayer structure found in natural biological systems.…”
Section: ■ Introductionmentioning
confidence: 99%
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“…Electron microscopy has shown that Aβ fibrils actively extract lipids from vesicle membranes through a detergent-like mechanism 50 . When multiple protein and membrane segments interact under amyloid promoting conditions, it has been shown that they form multi-lamellar suprastructures 51 . The protein assemblies line up with lipids in-between and the positively charged residues connect to the negatively charged lipids.…”
Section: Discussionmentioning
confidence: 99%
“…A number of studies have identified fibril-like assemblies of proteins with lipids in which the usual properties of amyloid fibrils are not observed. These proteins include some, such as lysozyme, that have previously described as amyloid forming ( 25 , 104 , 105 , 106 ), alongside nonamyloidogenic proteins with other forms of membrane activity, such as bovine seminal plasma protein PDC-109 ( 107 ) and temporin B, an antimicrobial peptide ( 49 ). The seminal peptide PAP(248–286) forms coaggregates with POPG that have some amyloid-like properties, such as binding thioflavin T, but otherwise differ from amyloid forms of the peptide in forming rapidly (<5 min) and being poor at seeding the growth of further amyloid fibrils ( 108 ).…”
Section: Evidence For the Presence Of Lipids In Amyloid Fibrilsmentioning
confidence: 99%