Temperature and pH effects on biophysical and morphological properties of self‐assembling peptide RADA16‐I

Ye, Zhaoyang; Zhang, Hangyu; Luo, Hanlin; Wang, Shunkang; Zhou, Qing‐han; Du, Xinzhong; Tang, Cheng-Wei; Chen, Liyan; Liu, Jingping; Shi, Yujun; Zhang, Eryong; Ellis-Behnke, Rutledge; Wang, Chao

doi:10.1002/psc.988

Cited by 109 publications

(107 citation statements)

References 42 publications

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“…When heated to 90°C, the self-assembled structure of R4 changes into aggregates ( Figure 5F). Previous study 31 has shown that RADA16-I exhibits β-sheet structure and forms unordered aggregates at 70°C, indicating that the nanostructure of R4 is more stable than that of RADA16-I.…”

Section: Stability Of Self-assembling Peptides R3 and R4mentioning

confidence: 85%

A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs

Sun¹,

Wang²

2012

IJN

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Mechanical strength of nanofiber scaffolds formed by the self-assembling peptide RADA16-I or its derivatives is not very good and limits their application. To address this problem, we inserted spidroin uncrystalline motifs, which confer incomparable elasticity and hydrophobicity to spider silk GGAGGS or GPGGY, into the C-terminus of RADA16-I to newly design two peptides: R3 (n-RADARADARADARADA-GGAGGS-c) and R4 (n-RADARADARADARADA-GPGGY-c), and then observed the effect of these motifs on biophysical properties of the peptide. Atomic force microscopy, transmitting electron microscopy, and circular dichroism spectroscopy confirm that R3 and R4 display β-sheet structure and self-assemble into long nanofibers. Compared with R3, the β-sheet structure and nanofibers formed by R4 are more stable; they change to random coil and unordered aggregation at higher temperature. Rheology measurements indicate that novel peptides form hydrogel when induced by DMEM, and the storage modulus of R3 and R4 hydrogel is 0.5 times and 3 times higher than that of RADA16-I, respectively. Furthermore, R4 hydrogel remarkably promotes growth of liver cell L02 and liver cancer cell SMCC7721 compared with 2D culture, determined by MTT assay. Novel peptides still have potential as hydrophobic drug carriers; they can stabilize pyrene microcrystals in aqueous solution and deliver this into a lipophilic environment, identified by fluorescence emission spectra. Altogether, the spider fibroin motif GPGGY most effectively enhances mechanical strength and hydrophobicity of the peptide. This study provides a new method in the design of nanobiomaterials and helps us to understand the role of the amino acid sequence in nanofiber formation.

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Section: Stability Of Self-assembling Peptides R3 and R4mentioning

confidence: 85%

A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs

Sun¹,

Wang²

2012

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“…According to the study by Z. Ye and X. Zhao et al, the random coils and β-turn of (RADA) 4 via hydrogen or ionic bonds would directly affect the stability of the β-sheet and nanofibers. 40 Thus, it is necessary to compare the β-sheet content with the random coils and β-turn. On the basis of this, the β/TR ratios have been calculated and compared, which supported that 25% v/v nanoparticle solution in hydrogel did not drastically affect the assembly of (RADA) 4 .…”

Section: Discussionmentioning

confidence: 99%

“…The chitosan nanoparticles were hard to distinguish from fiber A typical CD spectrum of (RADA) 4 β-sheet structure contains a minimum at ∼216 nm (β-sheet contents) and a maximum at 196 nm (the degree of β-sheet twist). 40 The nanoparticle solutions do not have absorption in CD examination, see Figure S2.…”

Section: Nanoparticle Characterization: Effect Of Phmentioning

confidence: 99%

pH-Triggered Release of Hydrophobic Molecules from Self-Assembling Hybrid Nanoscaffolds

Lü

Unsworth

2016

Biomacromolecules

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Vous avez des questions? Nous pouvons vous aider. Pour communiquer directement avec un auteur, consultez la première page de la revue dans laquelle son article a été publié afin de trouver ses coordonnées. Si vous n'arrivez pas à les repérer, communiquez avec nous à PublicationsArchive-ArchivesPublications@nrc-cnrc.gc.ca. Questions? Contact the NRC Publications Archive team atPublicationsArchive-ArchivesPublications@nrc-cnrc.gc.ca. If you wish to email the authors directly, please see the first page of the publication for their contact information. NRC Publications Archive Archives des publications du CNRCThis publication could be one of several versions: author's original, accepted manuscript or the publisher's version. / La version de cette publication peut être l'une des suivantes : la version prépublication de l'auteur, la version acceptée du manuscrit ou la version de l'éditeur. For the publisher's version, please access the DOI link below./ Pour consulter la version de l'éditeur, utilisez le lien DOI ci-dessous.http://doi.org/10.1021/acs.biomac.6b00040Access and use of this website and the material on it are subject to the Terms and Conditions set forth at pH-triggered release of hydrophobic molecules from self-assembling hybrid nanoscaffolds Lu, Lei; Unsworth, Larry D.http://nparc.cisti-icist.nrc-cnrc.gc.ca/fra/droits L'accès à ce site Web et l'utilisation de son contenu sont assujettis aux conditions présentées dans le site LISEZ CES CONDITIONS ATTENTIVEMENT AVANT D'UTILISER CE SITE WEB. NRC Publications Record / Notice d'Archives des publications de CNRC:http://nparc.cisti-icist.nrc-cnrc.gc.ca/eng/view/object/?id=9e4287db-e138-42bd-a2f4-805f4418351b http://nparc.cisti-icist.nrc-cnrc.gc.ca/fra/voir/objet/?id=9e4287db-e138-42bd-a2f4-805f4418351b pH-Triggered Release of Hydrophobic Molecules from SelfAssembling Hybrid Nanoscaffolds Lei Lu †, ‡ and Larry D. Unsworth* , †, ‡ † Department of Chemical and Materials Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada ‡ National Institute for Nanotechnology, National Research Council (Canada), Edmonton, Alberta T6G 2M9, Canada * S Supporting Information ABSTRACT: Self-assembling peptide based hydrogels have a wide range of applications in the field of tissue repair and tissue regeneration. Because of its physicochemical properties, (RADA) 4 has been studied as a potential platform for 3D cell culture, drug delivery, and tissue engineering. Despite some small molecule and protein release studies with this system, there is a lack of work investigating the controlled release of hydrophobic compounds (i.e., anti-inflammatory, anticancer, antibacterial drugs, etc.) that are important for many clinical therapies. Attempts to incorporate hydrophobic compounds into self-assembling matrices usually inhibited nanofiber formation, rather resulting in a peptide−drug complex or microcrystal formation. Herein, a selfassembling chitosan/carboxymethyl-β-cyclodextrin nanoparticle system was used to load dexamethasone, which formed within a self-assembling (RADA...

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“…From the circular dichroism analysis, the RADA16 peptide had a typical β-sheet structure (minimum molar ellipticity at 215-217 nm and maximum at 195-206 nm), with 50.6% β-sheet content ( Figure 3 and Table 1, S (r) + S [d]) according to the CDPro software analysis. 19 However, when RADA16 was stirred with PTX for 48 hours, there was an approximately 18.4% decrease in the β-sheet content and a 19.8% increase in the unordered structure content. Dynamic light scattering measurements showed that the diameter of nanofibers from a pure RADA16 solution was in the range of 10-50 nm.…”

Section: Interaction Of Rada16 and Ptxmentioning

confidence: 96%

Controlled release of paclitaxel from a self-assembling peptide hydrogel formed in situ and antitumor study in vitro

Liu¹

2011

IJN

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Background A nanoscale injectable in situ-forming hydrogel drug delivery system was developed in this study. The system was based on a self-assembling peptide RADA16 solution, which can spontaneously form a hydrogel rapidly under physiological conditions. We used the RADA16 hydrogel for the controlled release of paclitaxel (PTX), a hydrophobic antitumor drug. Methods The RADA16-PTX suspension was prepared simply by magnetic stirring, followed by atomic force microscopy, circular dichroism analysis, dynamic light scattering, rheological analysis, an in vitro release assay, and a cell viability test. Results The results indicated that RADA16 and PTX can interact with each other and that the amphiphilic peptide was able to stabilize hydrophobic drugs in aqueous solution. The particle size of PTX was markedly decreased in the RADA16 solution compared with its size in water. The RADA16-PTX suspension could form a hydrogel in culture medium, and the elasticity of the hydrogel showed a positive correlation with peptide concentration. In vitro release measurements indicated that hydrogels with a higher peptide concentration had a longer half-release time. The RADA16-PTX hydrogel could effectively inhibit the growth of the breast cancer cell line, MDA-MB-435S, in vitro, and hydrogels with higher peptide concentrations were more effective at inhibiting tumor cell proliferation. The RADA16-PTX hydrogel was effective at controlling the release of PTX and inhibiting tumor cell growth in vitro. Conclusion Self-assembling peptide hydrogels may work well as a system for drug delivery.

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Temperature and pH effects on biophysical and morphological properties of self‐assembling peptide RADA16‐I

Cited by 109 publications

References 42 publications

A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs

A self-assembling peptide RADA16-I integrated with spider fibroin uncrystalline motifs

pH-Triggered Release of Hydrophobic Molecules from Self-Assembling Hybrid Nanoscaffolds

Controlled release of paclitaxel from a self-assembling peptide hydrogel formed in situ and antitumor study in vitro

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