Functional metabolite assemblies—a review

Aizen, Ruth; Tao, Kai; Rencus‐Lazar, Sigal; Gazit, Ehud

doi:10.1007/s11051-018-4217-3

Cited by 26 publications

(23 citation statements)

References 39 publications

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“…Finally, another interesting parallelism can be found between protein and metabolite amyloids in the sense that as with protein amyloids, functional assemblies that are composed of metabolites can be formed. 352 One key example is the formation of tapetum lucidum, a retroreflector layer that facilitates night vision. These assemblies are formed by simple metabolites that are very similar to major human risk elements, including a nucleobase (guanine) in reptiles, an amino acid (cysteine coordinated with zinc) in dogs, and a vitamin (riboflavin) in cats and lemurs.…”

Section: Metabolite Amyloidosismentioning

confidence: 99%

Half a century of amyloids: past, present and future

et al. 2020

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Section: Metabolite Amyloidosismentioning

confidence: 99%

Half a century of amyloids: past, present and future

et al. 2020

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“…1,2 Functional metabolites assemblies, which originate from the higher-order supramolecular packing of simplest metabolite building blocks, are also abundant in nature. 3 An important example is the photonic structures observed in biological systems which are comprised of a regular array of layered metabolite crystals. 4 The shiny mirrorreflecting eyes of numerous animals result from the presence of assembled metabolites in the tapetum lucidum tissue which reflect light as well as divert it into a more useful range by fluorescence.…”

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Deciphering the Rules for Amino Acid Co-Assembly Based on Interlayer Distances

et al. 2019

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Metabolite materials are extremely useful to obtain functional bioinspired assemblies with unique physical properties for various applications in the fields of material science, engineering, and medicine by selfassembly of the simplest biological building blocks. Supramolecular co-assembly has recently emerged as a promising extended approach to further expand the conformational space of metabolite assemblies in terms of structural and functional complexity. Yet, the design of synergistically co-assembled amino acids to produce tailormade functional architectures is still challenging. Herein, we propose a design rule to predict the supramolecular coassembly of naturally occurring amino acids based on their interlayer separation distances observed in single crystals. Using diverse experimental techniques, we demonstrate that amino acids with comparable interlayer separation strongly interact and co-assemble to produce structural composites distinctly different from their individual properties. However, such an interaction is hampered in a mixture of differentially layer-separated amino acids, which self-sort to generate individual characteristic structures. This study provides a different paradigm for the modular design of supramolecular assemblies based on amino acids with predictable properties.

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“…[1][2][3] More recently, however, amyloid-forming peptide and protein building blocks have been increasingly discovered in functional roles in a range of organisms. [4,5] This finding has given inspiration for efforts focused on exploring the application of amyloids for artificial functional bio-inspired materials. [4,[6][7][8] In this context, short peptides with predictable and defined assembly behavior have emerged as potential building blocks for the generation of a versatile set of functional materials.…”

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“…Typically, well-ordered β-sheet-rich fibrils are formed by several filaments twisted in a rope-like manner; however, environmental factors can lead to heterogeneity of the assembled structural species. [5,19] Thus, stimuli-responsive behavior can be induced via modulation of solution environmental conditions to be further harnessed to allow fine-tuning of the assemblies properties and functionality. [20,21] In this study, we demonstrate that the inherent parameters governing peptide self-assembly can be harnessed and controlled by droplet microfluidic techniques to allow for micro and nanoscale structuring approaches.…”

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pH‐Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide

Shimanovich

Levin

Eliaz

et al. 2021

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of highly ordered, linear amyloids fibrils. Amyloids have originally been associated with neurodegenerative disorders. [1][2][3] More recently, however, amyloid-forming peptide and protein building blocks have been increasingly discovered in functional roles in a range of organisms. [4,5] This finding has given inspiration for efforts focused on exploring the application of amyloids for artificial functional bio-inspired materials. [4,[6][7][8] In this context, short peptides with predictable and defined assembly behavior have emerged as potential building blocks for the generation of a versatile set of functional materials. [9][10][11] Moreover, the chemical space offered by the possible amino acid sequences can be further expanded using genetic engineering and chemical functionalisation to allow peptide self-assembly and structural properties to be tailored to present specific properties and functionalities. [12][13][14][15][16] Amyloid and amyloid-like fibrils formed by a range of very different proteins and peptides present considerable similarity in their overall structural and morphological properties even when their sequence shows no common features. [17,18] This observation has given rise to the idea that the amyloid state can be a generally accessible for polypeptide chains and as such, molecular assemblies could be designed by optimizing the chemical composition of the peptide building blocks and their Peptides and proteins have evolved to self-assemble into supramolecular entities through a set of non-covalent interactions. Such structures and materials provide the functional basis of life. Crucially, biomolecular assembly processes can be highly sensitive to and modulated by environmental conditions, including temperature, light, ionic strength and pH, providing the inspiration for the development of new classes of responsive functional materials based on peptide building blocks. Here, it is shown that the stimuli-responsive assembly of amyloidogenic peptide can be used as the basis of environmentally responsive microcapsules which exhibit release characteristics triggered by a change in pH. The microcapsules are biocompatible and biodegradable and may act as vehicles for controlled release of a wide range of biomolecules. Cryo-SEM images reveal the formation of a fibrillar network of the capsule interior with discrete compartments in which cargo molecules can be stored. In addition, the reversible formation of these microcapsules by modulating the solution pH is investigated and their potential application for the controlled release of encapsulated cargo molecules, including antibodies, is shown. These results suggest that the approach described here represents a promising venue for generating pH-responsive functional peptide-based materials for a wide range of potential applications for molecular encapsulation, storage, and release.

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Functional metabolite assemblies—a review

Cited by 26 publications

References 39 publications

Half a century of amyloids: past, present and future

Half a century of amyloids: past, present and future

Deciphering the Rules for Amino Acid Co-Assembly Based on Interlayer Distances

pH‐Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide

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