Self-assembled peptide-based nanostructures, comprised of naturally occurring amino acids, display excellent biocompatibility, biodegradability, flexible responsiveness, and synthetic feasibility and can be customized for various biomedical applications. However, the lack of...
Fluorescent nanostructures obtained from small organic molecules or generated from supramolecular assembly of various functional π- conjugated molecules have concerned significant importance due to their potential applications in colour tunable...
A newly synthesized short peptide PS1 at different concentrations self-assemble into different nanostructures with various morphologies. The spherical units formed at lower concentration, considered as a potential candidate for intracellular delivery.
Two newly synthesized peptides, PA1 and PA2 with fluorinated aromatic unit and dicarboxylate group as an anchoring moiety able to form a non-toxic, stable, coating by a simple drop-coating method, improving the antifouling property of the surface.
Development of drug carriers, which
can chaperone xenobiotics directly
to their site of action, is an essential step for the advancement
of precision medicine. Cationic nanoparticles can be used as a drug
delivery platform for various agents including chemotherapeutics,
oligonucleotides, and antibodies. Self-assembly of short peptides
facilitates the formation of well-defined nanostructures suitable
for drug delivery, and varying the polarity of the self-assembly medium
changes the nature of noncovalent interactions in such a way as to
generate numerous unique nanostructures. Here, we have synthesized
an ultrashort cell-penetrating tetrapeptide (sequence Lys-Val-Ala-Val),
with Lys as a cationic amino acid, and studied the self-assembly property
of the BOC-protected (L1) and -deprotected (L2) analogues. Spherical
assemblies obtained from L1/L2 in a 1:1 aqueous ethanol system have
the ability to encapsulate small molecules and successfully enter
into cells, thus representing them as potential candidates for intracellular
drug delivery. To verify the efficacy of these peptides in the facilitation
of drug efficacy, we generated encapsulated versions of the chemotherapeutic
drug doxorubicin (Dox). L1- and L2-encapsulated Dox (Dox-L1 and Dox-L2),
similar to the unencapsulated drug, induced upregulation of regulator
of G protein signaling 6 (RGS6) and Gβ5, the critical mediators
of ATM/p53-dependent apoptosis in Dox-treated cancer cells. Further,
Dox-L1/L2 damaged DNA, triggered oxidative
stress and mitochondrial dysfunction, compromised cell viability,
and induced apoptosis. The ability of Dox-L1 to mediate cell death
could be ameliorated via knockdown of either RGS6 or Gβ5, comparable
to the results obtained with the unencapsulated drug. These data provide
an important proof of principle, identifying L1/L2 as drug delivery
matrices.
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