Synergistic Interactions Are Prevalent in Catalytic Amyloids

Marshall, Liam R.; Jayachandran, Megha; Lengyel‐Zhand, Zsofia; Rufo, Caroline M.; Kriews, Austin; Kim, Min Chul; Korendovych, Ivan V.

doi:10.1002/cbic.202000205

Cited by 11 publications

(11 citation statements)

References 39 publications

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“…The relative location of the residues in respect to the termini in the β‐hairpin does not affect the catalytic efficiency, as both t^QR and t^RQ demonstrate identical values, although their k cat and K M parameters differ slightly. This finding validates our previously reported model that assumed random distribution of the strand without a preference for particular arrangements of strands [4,8] …”

Section: Resultssupporting

confidence: 91%

“…Consistent with the results observed for the glutamine containing peptides, we saw a uniform drop in activity in all macrocycles relative to the heptapeptide assemblies in all cases, irrespective of the parallel or antiparallel orientation of the strands. Importantly, the mixed arginine‐tyrosine macrocycle (mRY) showed activity substantially higher than those of mRR and mYY, again demonstrating that the synergistic interactions previously identified in peptide mixtures persist in highly constrained environments [4,8] . Relatively minor sequence changes can have quite significant impact on the morphology of the peptide assemblies.…”

Section: Resultsmentioning

confidence: 83%

“…Most importantly, we have observed substantial positive synergistic interactions when mixing peptides with different sequences (Figure 1). [4,8] This finding shows how combinatorial screening of multiple functional groups can be done in a single fibril without the need for the covalent preparation of all possible amino acid combinations, which is fundamentally impossible.…”

Section: Introductionmentioning

confidence: 99%

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Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids

et al. 2020

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The self‐assembly of short peptides into catalytic amyloid‐like nanomaterials has proven to be a powerful tool in both understanding the evolution of early proteins and identifying new catalysts for practically useful chemical reactions. Here we demonstrate that both parallel and antiparallel arrangements of β‐sheets can accommodate metal ions in catalytically productive coordination environments. Moreover, synergistic relationships, identified in catalytic amyloid mixtures, can be captured in macrocyclic and sheet‐loop‐sheet species, that offer faster rates of assembly and provide more complex asymmetric arrangements of functional groups, thus paving the way for future designs of amyloid‐like catalytic proteins. Our findings show how initial catalytic activity in amyloid assemblies can be propagated and improved in more‐complex molecules, providing another link in a complex evolutionary chain between short, potentially abiotically produced peptides and modern‐day enzymes.

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 83%

Section: Introductionmentioning

confidence: 99%

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Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids

et al. 2020

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“…Finally, amyloids show another remarkable feature ‐ a potential for synergistic interactions (as well as antagonistic ones). For example, positively charged peptides co‐assembled favorably with negatively or neutral peptides, thus resulting in heteromeric assemblies that contain different functional groups [76] . Such heteromeric assemblies obviously possess higher structural complexity compared to homomeric ones, and thus present a potential for promoting more complex biochemical functions.…”

Section: Self‐assembly In Amyloid Fibersmentioning

confidence: 99%

Proto‐proteins in Protocells

Despotović

Tawfik

2021

ChemSystemsChem

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Phase separation, and coacervates in particular, may have played a key role in the transition from an abiotic to a biotic world, in providing early membrane‐less compartments and promoting metabolism. Herein, we highlight another potential role of coacervates in providing the milieu in which short abiotically formed peptides evolved gradually into structured, functional proteins. Coacervates, amyloids, and other rudimentary forms of self‐assembly enable short peptides to form supramolecular structures, thus providing the level of structural pre‐organization and complexity needed for biochemical function. Coacervates, however, are unique in also enabling co‐assembly of peptides and nucleic acids, and in promoting the acquisition of helical structures. These two properties, combined with their potential to promote the synthesis of biopolymers, make coacervates a feasible springboard for the emergence of the early nucleic acids binding proteins. Herein, we outline this putative evolutionary scenario and the evidence supporting it, also regarding the emergence of cationic amino acids that are critical to coacervate formation.

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“…These residues can affect the final amyloid conformation, the catalytic rates or the type of activity itself, though the interplay between these factors is far from clear. Furthermore, combinations of different peptides can result in synergistic interactions [51]. Peptides with the sequence LHLHLXL (in which X is replaced by different amino acids) form amyloids with diverse catalytic efficiencies that directly depend on the non-catalytic X residue.…”

Section: Catalytic Activity Emerging From Peptides Self-assembled Into Amyloidsmentioning

confidence: 99%

Catalytic Amyloids as Novel Synthetic Hydrolases

Duran-Meza

Díaz-Espinoza

2021

IJMS

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Amyloids are supramolecular assemblies composed of polypeptides stabilized by an intermolecular beta-sheet core. These misfolded conformations have been traditionally associated with pathological conditions such as Alzheimer’s and Parkinson´s diseases. However, this classical paradigm has changed in the last decade since the discovery that the amyloid state represents a universal alternative fold accessible to virtually any polypeptide chain. Moreover, recent findings have demonstrated that the amyloid fold can serve as catalytic scaffolds, creating new opportunities for the design of novel active bionanomaterials. Here, we review the latest advances in this area, with particular emphasis on the design and development of catalytic amyloids that exhibit hydrolytic activities. To date, three different types of activities have been demonstrated: esterase, phosphoesterase and di-phosphohydrolase. These artificial hydrolases emerge upon the self-assembly of small peptides into amyloids, giving rise to catalytically active surfaces. The highly stable nature of the amyloid fold can provide an attractive alternative for the design of future synthetic hydrolases with diverse applications in the industry, such as the in situ decontamination of xenobiotics.

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Synergistic Interactions Are Prevalent in Catalytic Amyloids

Cited by 11 publications

References 39 publications

Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids

Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids

Proto‐proteins in Protocells

Catalytic Amyloids as Novel Synthetic Hydrolases

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