Self-assembly of Surfactant-like Peptides with Variable Glycine Tails to Form Nanotubes and Nanovesicles

Santoso, Steve; Hwang, Wonmuk; Hartman, Hyman; Zhang, Shuguang

doi:10.1021/nl025563i

Cited by 325 publications

(332 citation statements)

References 36 publications

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“…As pointed out by Fishkis [19], the first cellular membranes may have consisted of polypeptides, possibly in conjunction with other prebiotic amphiphilic molecules. This idea is supported by findings indicating that short peptides can aggregate into fibrils, microtubes, and vesicles [52,53,60,70].…”

Section: Introductionmentioning

confidence: 64%

“…In contrast to the perspective provided by proponents of the lipid-world scenario [61], self-organization of short peptides has recently been proposed as a possible alternative to lipid self-organization for formation of the first protocellular membrane structures [19,60]. Although phospholipids are the primary components of modern cellular membranes, it is unlikely that such compounds were prevalent enough on the early Earth to be major components of the very first membranes [15,36].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Toward Homochiral Protocells in Noncatalytic Peptide Systems

Gleiser

Walker

2009

Orig Life Evol Biosph

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The activation-polymerization-epimerization-depolymerization (APED) model of Plasson et al. has recently been proposed as a mechanism for the evolution of homochirality on prebiotic Earth. The dynamics of the APED model in two-dimensional spatially-extended systems is investigated for various realistic reaction parameters. It is found that the APED system allows for the formation of isolated homochiral proto-domains surrounded by a racemate. A diffusive slowdown of the APED network induced, for example, through tidal motion or evaporating pools and lagoons leads to the stabilization of homochiral bounded structures as expected in the first self-assembled protocells.

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Section: Introductionmentioning

confidence: 64%

Section: Introductionmentioning

confidence: 99%

Toward Homochiral Protocells in Noncatalytic Peptide Systems

Gleiser

Walker

2009

Orig Life Evol Biosph

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“…Therefore, fractal nature may be strongly indicative of both the substrate-enzyme interaction and the diffusion within a matrix. One commonly used technique for classifying a fractal is the Hausdorff dimension analysis, which is an image-based technique employed to observe common patterns in otherwise random cell growth, laminin polymerization, nanotubes and nanovesicles, and other β-sheet forming SAPs [21,[31][32][33][34][35][36]. Despite its wide use, no fractal network has been observed in (RADA)4, nor has it been linked to differences in growth or the addition of cleavage sites for drug release.…”

Section: Introductionmentioning

confidence: 99%

Towards Developing Bioresponsive, Self-Assembled Peptide Materials: Dynamic Morphology and Fractal Nature of Nanostructured Matrices

Koss

Unsworth

2018

Preprint

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Abstract(RADA)4 nanoscaffolds are excellent candidates for use as peptide delivery vehicles: they are relatively easy to synthesize with custom bio-functionality, and assemble in situ to allow a focal point of release. This enables (RADA)4 to be utilized in multiple release strategies by embedding a variety of bioactive molecules in an all-in-one 'construct'. One novel strategy focuses on the local, on-demand release of peptides triggered via proteolysis of tethered peptide sequences. However, the spatial-temporal morphology of self-assembling nanoscaffolds may greatly influence the ability for enzymes to both diffuse into as well as actively cleave substrates. Fine structure and its impact on overall affect on peptide release is poorly understood. In addition, fractal networks observed in nanoscaffolds are linked to the fractal nature of diffusion in these systems. Therefore, matrix morphology and fractal dimension of virgin (RADA)4 and mixtures of (RADA)4 and matrix metalloproteinase 2 (MMP-2) cleavable substrate modified (RADA)4 were characterized over time. Sites of high (GPQG+IASQ, CP1) and low (GPQG+PAGQ, CP2) cleavage activity were chosen. Fine structure was visualized using established according to established methods. After 2 hrs of incubation, nanofiber networks showed an established fractal nature, however nanofibers continued to bundle in all cases as incubation times increased. It was observed that despite extensive nanofiber bundling after 24 hrs of incubation time, the CP1 and CP2 nanoscaffolds were susceptible to MMP-2 cleavage. The properties of these engineered nanoscaffolds characterized herein illustrate that they are an excellent candidate as an enzymatically initiated peptide delivery platform. Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 23 July 2018doi:10.20944/preprints201807.0435.v1Peer-reviewed version available at Materials 2018, 11, 1539; doi:10.3390/ma11091539 3 Keywords: Self-assembling peptides, RADA16, (RADA)4, MMP-2, Nanoscaffold, Hausdorff dimension, Fractal Statement of SignificanceThe (RADA)4 peptide sequence boasts major benefits over other drug delivery systems: it is capable of forming a focal point of diffusion that houses and releases a variety of ligands in physiological conditions, and it is simple to add other functionally degradable peptide motifs during a one-step synthesis. As such, we added protease cleavable sites cued to injury to create a novel delivery system. However, the addition of peptides may inhibit the desired self-assembly of these nanoscaffolds. In our study we addressed this concern by observing nanoscale architecture and fractal features during self-assembly, which have been linked to diffusion in similar scaffolds. We also demonstrated that these materials can degrade with the hypothesized proteolytic cues.Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted:

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“…[14][15][16][17] For example, peptides with a hydrophilic head and a hydrophobic tail spontaneously self-assemble to form vesicular structures in aqueous solution. 18 Peptide aggregation may alter the overall conformation and presentation of the amino acid sequence that interacts with cell surface receptors, which adversely affects the osteoinductive potential of the peptide. Although the structure and activity of BMP-2 protein has been extensively investigated in vitro and in vivo, there is limited data on aggregation and nanostructure formation by osteogenic peptides in aqueous solution and its effect on osteogenesis.…”

Section: Introductionmentioning

confidence: 99%

Experimental and Computational Investigation of the Effect of Hydrophobicity on Aggregation and Osteoinductive Potential of BMP-2-Derived Peptide in a Hydrogel Matrix

Moeinzadeh

Barati²,

Sarvestani³

et al. 2015

Tissue Engineering Part A

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An attractive approach to reduce the undesired side effects of bone morphogenetic proteins (BMPs) in regenerative medicine is to use osteoinductive peptide sequences derived from BMPs. Although the structure and function of BMPs have been studied extensively, there is limited data on structure and activity of BMP-derived peptides immobilized in hydrogels. The objective of this work was to investigate the effect of concentration and hydrophobicity of the BMP-2 peptide, corresponding to residues 73-92 of the knuckle epitope of BMP-2 protein, on peptide aggregation and osteogenic differentiation of human mesenchymal stem cells encapsulated in a polyethylene glycol (PEG) hydrogel. The peptide hydrophobicity was varied by capping PEG chain ends with short lactide segments. The BMP-2 peptide with a positive index of hydrophobicity had a critical micelle concentration (CMC) and formed aggregates in aqueous solution. Based on simulation results, there was a slight increase in the concentration of free peptide in solution with 1000-fold increase in peptide concentration. The dose-osteogenic response curve of the BMP-2 peptide was in the 0.0005-0.005 mM range, and osteoinductive potential of the BMP-2 peptide was significantly less than that of BMP-2 protein even at 1000-fold higher concentrations, which was attributed to peptide aggregation. Further, the peptide or PEG-peptide aggregates had significantly higher interaction energy with the cell membrane compared with the free peptide, which led to a higher nonspecific interaction with the cell membrane and loss of osteoinductive potential. Conjugation of the BMP-2 peptide to PEG increased CMC and osteoinductive potential of the peptide whereas conjugation to lactide-capped PEG reduced CMC and osteoinductive potential of the peptide. Experimental and simulation results revealed that osteoinductive potential of the BMP-2 peptide is correlated with its CMC and the free peptide concentration in aqueous medium and not the total concentration.

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Self-assembly of Surfactant-like Peptides with Variable Glycine Tails to Form Nanotubes and Nanovesicles

Cited by 325 publications

References 36 publications

Toward Homochiral Protocells in Noncatalytic Peptide Systems

Toward Homochiral Protocells in Noncatalytic Peptide Systems

Towards Developing Bioresponsive, Self-Assembled Peptide Materials: Dynamic Morphology and Fractal Nature of Nanostructured Matrices

Experimental and Computational Investigation of the Effect of Hydrophobicity on Aggregation and Osteoinductive Potential of BMP-2-Derived Peptide in a Hydrogel Matrix

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