Self-assembling dipeptide-based nontoxic vesicles as carriers for drugs and other biologically important molecules

Naskar, Jishu; Roy, Subhasish; Joardar, Anindita; Das, Sumantra; Banerjee, Arindam

doi:10.1039/c1ob05757j

Cited by 45 publications

(26 citation statements)

References 91 publications

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“…The prototype of this new class of molecules is the short and well‐known diphenylalanine (FF) homopeptide . Through a combination of π–π stacking and hydrogen‐bonding, different method of preparation, specific pH values or solvent, FF is able to self‐organize in different kinds of nano and macro morphologies (hollow nanotubes, fibers, vesicles, metastable hydrogels or organogels). These nanostructures have been investigated for their mechanical, electrochemical and optical properties .…”

Section: Introductionmentioning

confidence: 99%

Structural Characterization of Self‐Assembled Tetra‐Tryptophan Based Nanostructures: Variations on a Common Theme

et al. 2018

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Over the years, a large number of multidisciplinary investigations has unveiled that the self-assembly of short peptides and even of individual amino acids can generate a variety of different biomaterials. In this framework, we have recently reported that polyethylene glycol (PEG) conjugates of short homopeptides, containing aromatic amino acids such as phenylalanine (Phe, F) and naphthylalanine (Nal), are able to form elongated fibrillary aggregates having interesting chemical and physical properties. We here extend these analyses characterizing the self-assembling propensity of PEG -W4, a PEG adduct of the tetra-tryptophan (W4) sequence. A comprehensive structural characterization of PEG -W4 was obtained, both in solution and at the solid state, through the combination of spectroscopic, microscopic, X-ray scattering and computational techniques. Collectively, these studies demonstrate that this peptide is able to self-assemble in fibrillary networks characterized by a cross β-structure spine. The present findings clearly demonstrate that aromatic residues display a general propensity to induce self-aggregation phenomenon, despite the significant differences in the physicochemical properties of their side chains.

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Section: Introductionmentioning

confidence: 99%

Structural Characterization of Self‐Assembled Tetra‐Tryptophan Based Nanostructures: Variations on a Common Theme

et al. 2018

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“…Banergi and coworkers developed stable nanovesicles (320 ± 50 nm) over a wide pH range (pH 2-12) and responsive to Ca +2 ions from dipeptides that contained a glutamic acid residue located at C-terminus and C4 lipoamino acid at N-terminus. The vesicles encapsulated fluorescent dye and doxorubicin and released them in the presence of calcium ions [115]. Modification of short peptides containing phenylalanine to constrain their conformation ensured sustained released from hydrogel delivery systems with improved mechanical properties.…”

Section: Short Peptidesmentioning

confidence: 99%

Recent advances in self-assembled peptides: Implications for targeted drug delivery and vaccine engineering

Eskandari

Guerin

Tóth

et al. 2017

Advanced Drug Delivery Reviews

308

220

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Self-assembled peptides have shown outstanding characteristics for vaccine delivery and drug targeting. Peptide molecules can be rationally designed to self-assemble into specific nanoarchitectures in response to changes in their assembly environment including: pH, temperature, ionic strength, and interactions between host (drug) and guest molecules. The resulting supramolecular nanostructures include nanovesicles, nanofibers, nanotubes, nanoribbons, and hydrogels and have a diverse range of mechanical and physicochemical properties. These molecules can be designed for cell-specific targeting by including adhesion ligands, receptor recognition ligands, or peptide-based antigens in their design, often in a multivalent display. Depending on their design, self-assembled peptide nanostructures have advantages in biocompatibility, stability against enzymatic degradation, encapsulation of hydrophobic drugs, sustained drug release, shear-thinning viscoelastic properties, and/or adjuvanting properties. These molecules can also act as intracellular transporters and respond to changes in the physiological environment. Furthermore, this class of materials has shown sequence- and structure-dependent impacts on the immune system that can be tailored to non-immunogenic for drug targeting, and immunogenic for vaccine delivery. This review explores self-assembled peptide nanostructures (beta sheets, alpha helices, peptide amphiphiles, amino acid pairing, elastin like polypeptides, cyclic peptides, short peptides, Fmoc peptides, and peptide hydrogels) and their application in vaccine delivery and drug targeting.

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“…Chirality is ubiquitous in biological system. [16][17][18] Controlling the chiral self-assembly of peptides into well-defined nanostructures and microstructures has promising applications in various fields, including cell scaffolds, 19,20 regenerative medicine, 21,22 drug delivery, 23,24 and catalysis. 25,26 However, due to the complex evolution of noncovalent forces, controlling the chiral self-assembly of peptide and finding potential applications still remain difficult.…”

Section: Funding Informationmentioning

confidence: 99%

Protamine‐induced condensation of peptide nanofilaments into twisted bundles with controlled helical geometry

Wang

Jia

Wang

et al. 2019

Journal of Peptide Science

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Chiral self‐assembly of peptides is of fundamental interest in the field of biology and material science. Protamine, an alkaline biomacromolecule which is ubiquitous in fish and mammalian, plays crucial roles in directing the helical twisting of DNA. Inspired by this, we reported a bioinspired pathway to direct the hierarchical chiral self‐assembly of a short synthetic dipeptide. The peptide could self‐assemble into negatively charged chiral micelles in water that spontaneously formed a nematic liquid crystalline phase. By incorporation with protamine, the micelles condensed with the protamine into large helical bundles with precisely controlled diameter. Furthermore, to simulate the intracellular environments, we investigated macromolecular crowding on the coassembly of peptide and protamine, which leads to the formation of much thinner helical structures. The results highlight the roles of highly charged biomacromolecules and macromolecular crowding on peptide self‐assembly, which are beneficial for the practical applications of self‐assembling peptides in biomedicine and sensing.

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Self-assembling dipeptide-based nontoxic vesicles as carriers for drugs and other biologically important molecules

Cited by 45 publications

References 91 publications

Structural Characterization of Self‐Assembled Tetra‐Tryptophan Based Nanostructures: Variations on a Common Theme

Structural Characterization of Self‐Assembled Tetra‐Tryptophan Based Nanostructures: Variations on a Common Theme

Recent advances in self-assembled peptides: Implications for targeted drug delivery and vaccine engineering

Protamine‐induced condensation of peptide nanofilaments into twisted bundles with controlled helical geometry

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