Cell-penetrating peptides (CPPs) are crucial for delivering macromolecules such as nucleic acids into cells. This study investigates the effectiveness of dual-modified penetratin peptides, focusing on the impact of stapling structures and an endosomal escape domain (EED) on enhancing intracellular uptake. Some CPPs were synthesized with an EED at either the N- or C-terminus and stapling structures, and then complexed with plasmid DNA (pDNA) to evaluate their cellular uptake.
View Article and Find Full Text PDFIntroduction: Peptide foldamers play a critical role in pharmaceutical research and biomedical applications. This review highlights recent (post-2020) advancements in novel foldamers, synthetic techniques, and their applications in pharmaceutical research.
Areas Covered: The authors summarize the structures and applications of peptide foldamers such as α, β, γ-peptides, hydrocarbon-stapled peptides, urea-type foldamers, sulfonic-γ-amino acid foldamers, aromatic foldamers, and peptoids, which tackle the challenges of traditional peptide drugs.
Cell-penetrating peptides (CPPs) are widely used for the intracellular delivery of a variety of cargo molecules, including small molecules, peptides, nucleic acids, and proteins. Many cationic and amphiphilic CPPs have been developed; however, there have been few reports regarding hydrophobic CPPs. Herein, we have developed stapled hydrophobic CPPs based on the hydrophobic CPP, TP10, by introducing an aliphatic carbon side chain on the hydrophobic face of TP10.
View Article and Find Full Text PDFThe structural, electronic, and optical properties of the protected Au clusters with icosahedral (Ih) and face-centered cubic (FCC)-like Au cores were studied to understand the origin of the difference in the optical gaps of these clusters. It has been demonstrated that the choice of density functionals does not qualitatively affect the properties of Au and Au clusters with Ih and FCC cores. The density of states, molecular orbitals, and natural charges were analyzed in detail using the B3LYP functional.
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