Peptide membranes in chemical evolution☆

Childers, W. Seth; Ni, Rong; Mehta, Anil; Lynn, David G.

doi:10.1016/j.cbpa.2009.09.027

Cited by 53 publications

(75 citation statements)

References 81 publications

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“…58). Most of these assemblies have an underlying repetitive β-sheet structure and are therefore closely related to, if not correctly classified as, amyloids.…”

Section: Peptide Membranesmentioning

confidence: 93%

“…The forces that drive the assembly of peptides into membranes and the structures themselves are also very different from the nonspecific hydrophobic driven assembly of lipid molecules and, based on the structural models, resemble more the specific nature of protein folding. 58 The ability of simple peptides to form enclosing structures is of prebiotic significance for the simple reason that there is no evidence that lipids were the first biological barriers. They are particularly interesting because, like other amyloids, peptide membranes can form from very short sequences and, due to their nearly unlimited chemical diversity, will have the potential activities of other amyloids and larger proteins.…”

Section: Peptide Membranesmentioning

confidence: 99%

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On the Possible Amyloid Origin of Protein Folds

Greenwald¹,

Riek²

2012

Journal of Molecular Biology

129

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“…58). Most of these assemblies have an underlying repetitive β-sheet structure and are therefore closely related to, if not correctly classified as, amyloids.…”

Section: Peptide Membranesmentioning

confidence: 93%

Section: Peptide Membranesmentioning

confidence: 99%

On the Possible Amyloid Origin of Protein Folds

Greenwald¹,

Riek²

2012

Journal of Molecular Biology

129

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“…[2] Alternatively,p eptide membranes have also been proposed to play ar ole in chemical evolution, not only through the formation of closedv esicles, but also through other morphologies, such as hollow tubes, ribbons, andf ibers. [3] In fact, in some recent reports, self-assembled fibrillar networks were advocated as the most applicable functional scaffolds for simple prebiotic systems. [4] Fibrillar networks are also found in today's cellulare nvironments, either as structural frameworks within the cell (i.e., actin), or as components of the extracellularm atrix.…”

Section: Introductionmentioning

confidence: 99%

Emergent Catalytic Behavior of Self‐Assembled Low Molecular Weight Peptide‐Based Aggregates and Hydrogels

Tena‐Solsona

Nanda

Díaz‐Oltra

et al. 2016

Chemistry A European J

122

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We report a series of short peptides possessing the sequence (FE)n or (EF)n and bearing l-proline at their N-terminus that self-assemble into high aspect ratio aggregates and hydrogels. We show that these aggregates are able to catalyze the aldol reaction, whereas non-aggregated analogues are catalytically inactive. We have undertaken an analysis of the results, considering the accessibility of catalytic sites, pKa value shifts, and the presence of hydrophobic pockets. We conclude that the presence of hydrophobic regions is indeed relevant for substrate solubilization, but that the active site accessibility is the key factor for the observed differences in reaction rates. The results presented here provide an example of the emergence of a new chemical property caused by self-assembly, and support the relevant role played by self-assembled peptides in prebiotic scenarios. In this sense, the reported systems can be seen as primitive aldolase I mimics, and have been successfully tested for the synthesis of simple carbohydrate precursors.

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“…13 for the C 14 (N-myristoyl) and C 16 (N-palmitoyl) assemblies, respectively. This ability to systematically control the laminate spacing by simply changing the length of the acyl chain offers an as yet inaccessible materials design element and it focused our attention on the complete characterization of the homogeneous N-lauroyl-Ab(16-22) tubes.Electron diffraction [13,15] (Figure 2 c, d) and simulations [16] (Supporting Information, Figure S2) from the top and bottom walls of oriented tubes [10,17] defined a distinct tilt angle of the Figure 1. a) Structure of N-lauroyl-Ab(16-22); b) TEM, cryo-SEM (inset), and c) AFM micrographs of 1.2 mm N-lauroyl-Ab(16-22) assembled in 40 % acetonitrile/water with 0.1 % trifluoroacetic acid for 1-2 weeks.…”

mentioning

confidence: 99%

“…Electron diffraction [13,15] (Figure 2 c, d) and simulations [16] (Supporting Information, Figure S2) from the top and bottom walls of oriented tubes [10,17] defined a distinct tilt angle of the Figure 1. a) Structure of N-lauroyl-Ab(16-22); b) TEM, cryo-SEM (inset), and c) AFM micrographs of 1.2 mm N-lauroyl-Ab(16-22) assembled in 40 % acetonitrile/water with 0.1 % trifluoroacetic acid for 1-2 weeks.…”

mentioning

confidence: 99%

Remodeling Cross‐β Nanotube Surfaces with Peptide/Lipid Chimeras

Childers

Hardcastle

et al. 2012

Angew Chem Int Ed

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Peptide/lipid chimeras, which are generally referred to as peptide amphiphiles, array specific peptides on the surface of ordered lipid assemblies. [1] These materials are being explored as tissue scaffolds, in drug delivery, as antimicrobrials, and for biomineralization applications. [2][3][4][5][6] However, the increasing realization that simple peptides with high cross-b fold propensity can achieve long-range ordered arrays comparable to lipid amphiphiles has now allowed for the creation of an entirely new architectural framework. This framework not only offers precisely controlled positioning of charges and hydrophobic patches along a robust nanotube surface, but also the systematic adjustment of that spacing in a manner that to this point has been unrealized in self-assembling materials.Peptide amphiphiles can achieve remarkable long-range order within a range of topological lipid phases. [2][3][4][5][6] For example, the elongated worm-like micelles have been modeled as having alkane interiors with peptide surfaces, [4] a morphology that reflects the same structural tension between head group and alkane that molds phospholipid assemblies. [5] This structure suggests that various self-assembling peptide elements might be able to extend the standard amphiphile tensions into new frameworks, and focused our attention on the strong self-organizing potential of the cross-b fold. [3,5,7,8] The nucleating core sequence of the amyloid forming Ab-peptide associated with Alzheimers disease, Ab(16-22), K 16 LVFFAE 22 -NH 2 , which organizes into diverse cross-b assemblies, [9][10][11][12][13] was acylated through conventional solid-phase Fmoc chemistry at the N-terminus with straightchain fatty acids ranging in length from two to sixteen carbon atoms. The products were purified by RP-HPLC, assembled under a range of conditions, and the resulting assemblies scored by electron microscopy (EM).Of the series assembled under acidic conditions, C 2 (Nacetyl) through C 4 (N-butyryl) assemblies were morpholog-ically indistinguishable (Supporting Information, Figure S1), and assigned as hollow tubes based on the previously characterized N-acetyl-Ab(16-22) assemblies. [10] Intermediate acyl chain lengths, C 5 to C 10 , assembled as ribbons, and longer lengths, C 14 and C 16 , formed fibers (Supporting Information, Figure S1). Most notably however, the C 11 (N-undecanoyl), C 12 (N-lauroyl), and C 13 (N-tridecanoyl) Ab(16-22) chimeras appeared as homogeneous tubes most similar to the N-acetyl assemblies, with the same distinct edges that arise from negative staining by uranyl acetate deposition inside and outside the tube cavity (Figure 1 b).High-resolution cryo-SEM further confirmed the Nlauroyl-Ab(16-22) assemblies as hollow nanotubes (Figure 1 b, inset) and the diameters of (56 AE 8) nm were also remarkably similar to the well-characterized N-acetyl-Ab(16-22) tubes. [10] Powder X-ray diffraction analyses [14] (Figure 2 a) gave sharp and distinct reflections for the H-bonded b-strand repeat at 4.7 for all acyl chain lengths, but ...

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Peptide membranes in chemical evolution☆

Cited by 53 publications

References 81 publications

On the Possible Amyloid Origin of Protein Folds

On the Possible Amyloid Origin of Protein Folds

Emergent Catalytic Behavior of Self‐Assembled Low Molecular Weight Peptide‐Based Aggregates and Hydrogels

Remodeling Cross‐β Nanotube Surfaces with Peptide/Lipid Chimeras

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