How do you design a peptide building block to make 2-dimentional nanowebs and 3-dimensional fibrous mats? This question has not been addressed with peptide self-assembling nanomaterials. This article describes a designed 9-residue peptide, N-Pro-Ser-Phe-CysPhe-Lys-Phe-Glu-Pro-C, which creates a strong fishnet-like nanostructure depending on the peptide concentrations and mechanical disruptions. This peptide is intramolecularly amphiphilic because of a single pair of ionic residues, Lys and Glu, at one end and nonionic residues, Phe, Cys, and Phe, at the other end. Circular dichroism and Fourier transform infrared spectroscopy analysis demonstrated that this peptide adopts stable -turn and -sheet structures and self-assembles into hierarchically arranged supramolecular aggregates in a concentration-dependent fashion, demonstrated by atomic force microscopy and electron microscopy. At high concentrations, the peptide dominantly self-assembled into globular aggregates that were extensively connected with each other to form ''beads-on-a-thread'' type nanofibers. These long nanofibers were extensively branched and overlapped to form a self-healing peptide hydrogel consisting of >99% water. This peptide can encapsulate the hydrophobic model drug pyrene and slowly release pyrene from coated microcrystals to liposomes. It can effectively stop animal bleeding within 30 s. We proposed a plausible model to interpret the intramolecular amphiphilic self-assembly process and suggest its importance for the future development of new biomaterials for drug delivery and regenerative medicine.-turn/-sheet ͉ hemostasis ͉ nanofibers ͉ hydrogel ͉ self-assembly D esign and fabrication of nanoscale biomaterials are critically important for the advancement of biomedical engineering. These include scaffolds for 3D cell and tissue culture, injured tissue repair, and controlled drug release. Biomaterials derived from synthetic or biological polymers have been used extensively for many biomedical applications over decades. Only recently, researchers have attempted to use structural motifs found in nature materials to design and fabricate nanobiomaterials for tissue engineering and regenerative medicine. It is known that many of fibrous proteins and peptides self-assemble into supramolecular structures by using -sheet structures, and one of the typical self-assembling peptides is the RADA16-I (1-9), termed as ionic self-complementary peptide. This kind of peptide has been designed by mimicking native protein motifs containing regular repeats of alternating oppositely charged residues separated by 1 or 2 hydrophobic residues. These residues interact with each other by at least three major forces: interand intramolecular forces such as hydrogen bonding, hydrophobic, and electrostatic interactions to drive molecular selfassembly process. Because charged amino acids play an important role in determining peptide molecular assembly through electrostatic interaction and hydrogen bonding, many of the self-assembling biomaterials are designed to ...
A novel
self-assembling peptide-functionalized
core–shell mesoporous silica nanoparticle was developed as
a drug carrier. Superparamagnetic manganese- and cobalt-doped iron
oxide nanoparticles formed the core for the mesoporous silica shell
coating. On the silica outer shell, the peptide Boc–Phe–Phe–Gly–Gly–COOH
was covalently conjugated by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
hydrochloride and N-hydroxysulfosuccinimide sodium
salt coupling. The self-assembling property of the peptide at physiological
temperature was utilized to block the pore openings, while the disassembly
at elevated local particle temperature released cargo molecules without
bulk heating that would cause cell damage. Both conventional heating
and heating in an alternating magnetic field were tested for the release
of fluorescein and daunorubicin. In vitro experiments showed high
cytotoxicity on pancreatic carcinoma cells (PANC-1) when this delivery
system was activated by an alternating magnetic field, while control
particles without drugs showed no obvious cytotoxicity.
In this study, an adjustable pH‐responsive drug delivery system using mesoporous silica nanoparticles (MSNs) as the host materials and the modified polypeptides as the nanovalves is reported. Since the polypeptide can self‐assemble via electrostatic interaction at pH 7.4 and be disassembled by pH changes, the modified poly(l‐lysine) and poly(l‐glutamate) are utilized for pore blocking and opening in the study. Poly(l‐lysine)‐MSN (PLL‐MSN) and poly(l‐glutamate)‐MSN (PLG‐MSN) are synthesized via the ring opening polymerization of N‐carboxyanhydrides onto the surface of mesoporous silica nanoparticles. The successful modification of the polypeptide on MSN is proved by Zeta potential change, X‐ray photoelectron spectroscopy (XPS), solid state NMR, and MALDI‐TOF MS. In vitro simulated dye release studies show that PLL‐MSN and PLG‐MSN can successfully load the dye molecules. The release study shows that the controlled release can be constructed at different pH by adjusting the ratio of PLL‐MSN to PLG‐MSN. Cellular uptake study indicates that the drug is detected in both cytoplasm and nucleus, especially in the nucleus. In vitro cytotoxicity assay indicates that DOX loaded mixture nanoparticles (ratio of PLL‐MSN to PLG‐MSN is 1:1) can be triggered for drug release in HeLa cells, resulting in 88% of cell killing.
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