Amphiphilic peptides as novel nanomaterials: design, self-assembly and application

Qiu, Feng; Chen, Yongzhu; Tang, Cheng-Wei; Wang, Chao

doi:10.2147/ijn.s166403

Cited by 81 publications

(45 citation statements)

References 130 publications

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“…This is different to the effect seen with alanine-based peptides, suggesting that the coupling with 1.9kDa PEG confers a high level of hydrophilicity, which can be balanced only by the higher hydrophobicity of valine compared to alanine residues. Moreover, PEGylation seems to induce the formation of more homogeneous and elongated micelles, unlike non-PEGylated octapeptides for which fibrillar or ribbon-like structures have been already reported [32][33][34] .…”

Section: Resultsmentioning

confidence: 88%

PEGylation affects the self-assembling behaviour of amphiphilic octapeptides

Perinelli

Campana

Singh

et al. 2019

International Journal of Pharmaceutics

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Surfactant-like peptides are a class of amphiphilic macromolecules, which are able to self-assemble in water forming different supramolecular structures. Among them, octapeptides composed of six hydrophobic and two hydrophilic residues have attracted interest since they have a length similar to those of natural phospholipids. Supramolecular structures of different amphiphilic octapeptides have been widely reported, but no study has been performed aimed at investigating the effect of PEGylation on their self-assembling behaviour. The aim of the present work was to synthesize and characterise the self-assembling behaviour of PEGylated alanine-or valine based amphiphilic octapeptides (mPEG1.9kDa-DDAAAAAA and mPEG1.9kDa-DDVVVVVV) in comparison to the non-PEGylated ones (DDAAAAAA and DDVVVVVV). The self-aggregation process in ultrapure water was investigated by fluorescence spectroscopy, small angle neutron scattering (SANS), dynamic light scattering (DLS), while the secondary structure was assessed by circular dichroism. PEGylation markedly affects the self-assembling behaviour of these amphiphilic octapeptides in terms of both critical aggregation concentration (CAC) and shape of the formed supramolecular aggregates. Indeed, PEGylation increases CAC and prevents the self-aggregation into fibrillary supramolecular aggregates (as observed for non-PEGylated peptides), by promoting the formation of micelle-like structures (as demonstrated for valine-based octapeptide). 2 On the other side, the secondary structure of peptides seems not to be affected by PEGylation. Overall, these results suggest that self-assembling behaviour of amphiphilic octapeptides can be modified by PEGylation, with a great potential impact for the future applications of these nanomaterials.

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Section: Resultsmentioning

confidence: 88%

PEGylation affects the self-assembling behaviour of amphiphilic octapeptides

Perinelli

Campana

Singh

et al. 2019

International Journal of Pharmaceutics

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“…In these approaches, hydrophobic domains are often introduced onto polymers for assembly into networks. While self‐assembly of peptide amphiphiles depend largely on hydrophobic interactions, these have been well reviewed elsewhere and we direct the reader to other reviews of interest on this topic …”

Section: Physical Associations To Assemble Hydrogelsmentioning

confidence: 99%

Recent advances in shear‐thinning and self‐healing hydrogels for biomedical applications

Uman

Dhand

Burdick

2019

J of Applied Polymer Sci

238

215

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Shear‐thinning and self‐healing hydrogels are being investigated in various biomedical applications including drug delivery, tissue engineering, and 3D bioprinting. Such hydrogels are formed through dynamic and reversible interactions between polymers or polypeptides that allow these shear‐thinning and self‐healing properties, including physical associations (e.g., hydrogen bonds, guest–host interactions, biorecognition motifs, hydrophobicity, electrostatics, and metal–ligand coordination) and dynamic covalent chemistry (e.g., Schiff base, oxime chemistry, disulfide bonds, and reversible Diels–Alder). Their shear‐thinning properties allow for injectability, as the hydrogel exhibits viscous flow under shear, and their self‐healing nature allows for stabilization when shear is removed. Hydrogels can be formulated as uniform polymer and polypeptide assemblies, as hydrogel nanocomposites, or in granular hydrogel form. This review focuses on recent advances in shear‐thinning and self‐healing hydrogels that are promising for biomedical applications. © 2019 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2020, 137, 48668.

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“…Besides surface functionalization with specific binding peptides, self-assemble peptide amphiphiles (PAs) have also been used for peptide-based GF immobilization (Hosseinkhani et al, 2006;Hsieh et al, 2006;Stupp et al, 2010). PAs are peptidebased molecules containing a hydrophilic tail and hydrophobic head composed of several amino acids, that mimic surfactant structures (Qiu et al, 2018). In order to confer biological activity to these peptides, they are conjugated to bioactive epitopes that are placed as the hydrophilic tail, since the hydrophobic head must be conserved to ensure the self-assembling process (Cui et al, 2010;Qiu et al, 2018).…”

Section: Peptide-based Immobilizationmentioning

confidence: 99%

Immobilization of Growth Factors for Cell Therapy Manufacturing

Enriquez-Ochoa

Robles-Ovalle

Mayolo‐Deloisa

et al. 2020

Front. Bioeng. Biotechnol.

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Cell therapy products exhibit great therapeutic potential but come with a deterring price tag partly caused by their costly manufacturing processes. The development of strategies that lead to cost-effective cell production is key to expand the reach of cell therapies. Growth factors are critical culture media components required for the maintenance and differentiation of cells in culture and are widely employed in cell therapy manufacturing. However, they are expensive, and their common use in soluble form is often associated with decreased stability and bioactivity. Immobilization has emerged as a possible strategy to optimize growth factor use in cell culture. To date, several immobilization techniques have been reported for attaching growth factors onto a variety of biomaterials, but these have been focused on tissue engineering. This review briefly summarizes the current landscape of cell therapy manufacturing, before describing the types of chemistry that can be used to immobilize growth factors for cell culture. Emphasis is placed to identify strategies that could reduce growth factor usage and enhance bioactivity. Finally, we describe a case study for stem cell factor.

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Amphiphilic peptides as novel nanomaterials: design, self-assembly and application

Cited by 81 publications

References 130 publications

PEGylation affects the self-assembling behaviour of amphiphilic octapeptides

PEGylation affects the self-assembling behaviour of amphiphilic octapeptides

Recent advances in shear‐thinning and self‐healing hydrogels for biomedical applications

Immobilization of Growth Factors for Cell Therapy Manufacturing

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