2016
DOI: 10.1039/c6nr03580a
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Bio-inspired metal ions regulate the structure evolution of self-assembled peptide-based nanoparticles

Abstract: We report an assembly and transformation process of a supramolecular module, BP-KLVFF-RGD (BKR) in solution and on specific living cell surfaces for imaging and treatment. The BKR self-assembled into nanoparticles, which further transformed into nanofibers in situ induced by coordination with Ca(2+) ions.

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Cited by 51 publications
(39 citation statements)
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“…The BKR initially self‐assembled into nanoparticles due to hydrophobic interactions, which further transformed into H bond stabilized nanofibers in situ induced by coordination with Ca 2+ . More importantly, the BKR nanoparticles could bind to U87 cell membrane through the interaction of RGD with Ca 2+ in α v β 3 integrins that result in morphology of BKR assemblies transformed from nanoparticles into nanofibers on U87 cell surfaces, leading to the cell death . Consequently, the same group constructed transformable NPs which could in situ transform into NFs and inhibit tumor invasion and metastasis in vivo.…”
Section: In Situ Constructed Peptide‐based Nanomaterialsmentioning
confidence: 84%
See 1 more Smart Citation
“…The BKR initially self‐assembled into nanoparticles due to hydrophobic interactions, which further transformed into H bond stabilized nanofibers in situ induced by coordination with Ca 2+ . More importantly, the BKR nanoparticles could bind to U87 cell membrane through the interaction of RGD with Ca 2+ in α v β 3 integrins that result in morphology of BKR assemblies transformed from nanoparticles into nanofibers on U87 cell surfaces, leading to the cell death . Consequently, the same group constructed transformable NPs which could in situ transform into NFs and inhibit tumor invasion and metastasis in vivo.…”
Section: In Situ Constructed Peptide‐based Nanomaterialsmentioning
confidence: 84%
“…Schematic representation of metal ion binding induced reconstruction of BKR nanoassemblies from nanoparticles to nanofibers in solution and on the cell surface. Reproduced with permission . Copyright 2016, Royal Society of Chemistry.…”
Section: In Situ Constructed Peptide‐based Nanomaterialsmentioning
confidence: 99%
“…Two absorption peaks centered at 265 and 480 nm appeared (Figure 1 A), representing the peptide backbone and DOX molecule, respectively, and the decrease in absorption over time revealed the formation of assembled aggregates. In particular, the absorbance at 265 nm decreased in a time-dependent manner, suggesting that DPC molecules aggregated through π-π interactions between aromatic residues 27 , 30 .…”
Section: Resultsmentioning
confidence: 99%
“…NIRF imaging was performed using a PE IVIS Spectrum imaging system for each group of mice at selected postinjection time points i.e. 0.5, 1, 2, 4, 6, 8, 10, 12, 18, 24, 36, 48, 60, 72 and 96 h. Three optical channels were recorded with selected excitation and emission bandpass filters 27 : Cy5.5 (λ ex =640 nm and λ em =720 nm); Cy7 (λ ex =745 and λ em = 800 nm); and FRET (λ ex =640 nm and λ em = 800 nm). The exposure time for each image was 0.1s.…”
Section: Methodsmentioning
confidence: 99%
“…In addition, the self‐assembly of the short peptides to nanofibers could be mediated by metal ion such as Ca 2+ if the peptides are coupled with RGD . RGD is reported to coordinate with metal ions like Ca 2+ and Mg 2+ and this coordination was confirmed to stabilize the hydrogen bond between the peptide molecules and is the driving force to induce fiber formation.…”
Section: Hydrogels and Nanofibersmentioning
confidence: 98%