ILQINS Hexapeptide, Identified in Lysozyme Left-Handed Helical Ribbons and Nanotubes, Forms Right-Handed Helical Ribbons and Crystals

Lara, Cécile; Reynolds, Nicholas P.; Berryman, Joshua T.; Xu, Anqiu; Zhang, Afang; Mezzenga, Raffaele

doi:10.1021/ja500445z

Cited by 89 publications

(144 citation statements)

References 64 publications

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“…Likewise, Lara et al recently found the shorter peptide sequence ILQINS to be highly amyloidogenic at room temperature. 53 This region of the protein is partially embedded inside the HEWL structure as a pocket in the junction connecting the α-domain and the β-domain. Combined with results from previous studies, our findings in this work indicated that the stability of this region in the β-domain directly determines the aggregation fate of the entire protein, dictating whether it proceeds to form amorphous aggregates or amyloid fibril.…”

Section: ■ Discussionmentioning

confidence: 99%

Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme

Wang

Chang

et al. 2014

J. Agric. Food Chem.

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Myricetin is a natural flavonol found in many grapes, berries, fruits, vegetables, and herbs as well as other plants. Recent studies have identified potential antiamyloidogenic activity for this compound. In this study, the kinetics of amyloid fibril formation by hen egg white lysozyme (HEWL) and the antifibril-forming activity of myricetin were investigated. We demonstrate that myricetin significantly inhibits the fibrillation of HEWL and the inhibitory effect is dose-dependent. Interestingly, the inhibitory effect toward HEWL fibrillation was stronger than that exerted by the previously characterized fibril-forming inhibitor quercetin, which has high structural similarity with myricetin. Spectrofluorometric and computational studies suggest that the mechanism underlying the inhibitory action of myricetin at a molecular level is to reduce the population of partially unfolded HEWL intermediates. This action is achieved by the tight binding of myricetin to the aggregation-prone region of the β-domain of HEWL and linking to the relatively stable α-domain, thus resulting in the inhibition of amyloid fibril formation. KEYWORDS: myricetin, lysozyme, amyloid, molecular dynamics simulation, molecular docking ■ INTRODUCTIONAmyloid diseases are characterized by conformational changes of certain proteins, which lead to intracellular or extracellular aggregation, eventually resulting in fibrillar amyloid deposits in the affected tissue. Currently there are approximately 30 extracellular fibril proteins known to be associated with human amyloidosis. 1 The so-called "hereditary non-neuropathic systemic amyloidosis" is associated with two lysozyme variants (I56T and D67H), which were identified in the early 1990s 2 and other naturally occurring amyloidogenic variants (F57I, F57I/ T70N, W64R, and T70N/W112R) discovered more recently. 3−5 The pathological characteristics of these amyloidoses includes the deposition of the full-length protein variants in organs, such as liver, spleen, and kidneys. 2 At present there are still no effective treatments for amyloid diseases such as Alzheimer's disease, systemic amyloidosis, familial amyloid polyneuropathy, and Creutzfeldt-Jakob disease, and all drugs in development that target Alzheimer's disease have failed at various stages of clinical trials. 6 However, the identification and development of small molecules that inhibit fibril formation by amyloidogenic proteins is a promising area of research. 7,8 Among the most promising small-molecule inhibitors, the naturally occurring polyphenols show the most effective antiamyloidogenic activity. 9 A group of polyphenols found in green tea (GTPs) including (−)-epigallocatechin (EGC), (−)-epicatechin gallate (ECG), and (−)-epigallocatechin gallate (EGCG) have been reported as effective inhibitors of alkali-saltinduced fibrillogenesis of hen egg white lysozyme (HEWL) with ECG as the most potent polyphenol. 10 A previous report demonstrated that curcumin can also inhibit the aggregation and formation of amyloid fibrillation of HEWL ...

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Section: ■ Discussionmentioning

confidence: 99%

Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme

Wang

Chang

et al. 2014

J. Agric. Food Chem.

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“…ForLPF hydrogel, negative Cotton effects were observed at 268 and 316 nm ( Figure 2a;S upporting Information, Figure S7a). LPF/Tb 3+ gel also exhibited two negative Cotton effects.Inthe presence of Li + ,N a + ,C o 2+ ,N i 2+ ,C u 2+ ,Z n 2+ ,C d 2+ ,M n 2+ ,M g 2+ ,C a 2+ , and Al 3+ metal ions,C Ds ignals remained profiles of plain LPF assembly (Supporting Information, Figure S8a,c), which are contrary with SEM results.T he reason may be that the terminal interaction of the gelators plays an important role in defining the morphology of the assemblies [10] and, in contrast, their characteristic CD signals without inversion was mainly determined by the chirality of phenylalanine. [11] Furthermore, CD signal intensities were different at the same equimolar concentration of different metal ions,i ndicating different coordination efficiencies.W eak CD signals were observed when metal ions such as Ag + ,Ba 2+ ,F e 3+ ,and Eu 3+ existed in LPF gels (Supporting Information, Figure S8b,d).…”

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confidence: 99%

Metal‐Ion‐Mediated Supramolecular Chirality of l‐Phenylalanine Based Hydrogels

Wang

Feng

2018

Angewandte Chemie

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Forchiral hydrogels and related applications,one of the critical issues is howtocontrol the chirality of supramolecular systems in an efficient way, including easy operation, efficient transfer of chirality,a nd so on. Herein, supramolecular chirality of l-phenylalanine based hydrogels can be effectively controlled by using abroad range of metal ions.The degree of twisting (twist pitch) and the diameter of the chiral nanostructures can also be efficiently regulated. These are ascribed to the synergic effect of hydrogen bonding and metal ion coordination. This study may develop am ethod to design an ew class of electronically,o ptically,a nd biologically active materials.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

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“…The fragment itself also forms fibrillar structures when incubated at room temperature and pH 2.0. Interestingly, the ribbons from this fragment show a right‐handed twist, whereas ribbons formed from LYS are left‐handed (Lara et al., ).…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

Jansens

Lambrecht

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Conditions including heating mode, time, temperature, pH, moisture and protein concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes, and/or salt influence amyloid fibril (AF) formation as they can affect the accessibility of amino acid sequences prone to aggregate. As some conditions applied on model protein resemble conditions in food processing unit operations, we here hypothesize that food processing can lead to formation of protein AFs with a compact cross β‐sheet structure. This paper reviews conditions and food constituents that affect amyloid fibrillation of egg and cereal proteins. While egg and cereal proteins often coexist in food products, their impact on each other's fibrillation remains unknown. Hen egg ovalbumin and lysozyme form AFs when subjected to moderate heating at acidic pH separately. AFs can also be formed at higher pH, especially in the presence of alcohols or chaotropic/reducing agents. Tryptic wheat gluten digests can form fibrillar structures at neutral pH and maize and rice proteins do so in aqueous ethanol or at acidic pH, respectively.

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ILQINS Hexapeptide, Identified in Lysozyme Left-Handed Helical Ribbons and Nanotubes, Forms Right-Handed Helical Ribbons and Crystals

Cited by 89 publications

References 64 publications

Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme

Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme

Metal‐Ion‐Mediated Supramolecular Chirality of l‐Phenylalanine Based Hydrogels

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

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