Oligonucleotide Delivery with Cell Surface Binding and Cell Penetrating Peptide Amphiphile Nanospheres

Mumcuoglu, Didem; Sardan, Melis; Tekinay, Turgay; Güler, Mustafa O.; Tekinay, Ayşe B.

doi:10.1021/acs.molpharmaceut.5b00007

Cited by 30 publications

(20 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Guler et al investigated multicomponent peptide amphiphile (PA)/oligonucleotide sytems for intracellular delivery of AONs. 622 PAs were designed that included N -terminal lauryl groups attached to a P 4 polyproline with C -terminal olignoculeotide-binding/cell penetrating motifs (Figure 49A). These self-assembling PAs were found to form spherical particles that bound AONs at the solvent exposed exterior face (Figure 49B).…”

Section: Peptide/biopolymer Hybridsmentioning

confidence: 99%

Multicomponent peptide assemblies

2018

View full text Add to dashboard Cite

Self-assembled peptide nanostructures have been increasingly exploited as functional materials for applications in biomedicine and energy. The emergent properties of these nanomaterials determine the applications for which they can be exploited. It has recently been appreciated that nanomaterials composed of multicomponent coassembled peptides often display unique emergent properties that have the potential to dramatically expand the functional utility of peptide-based materials. This review presents recent efforts in the development of multicomponent peptide assemblies. The discussion includes multicomponent assemblies derived from short low molecular weight peptides, peptide amphiphiles, coiled coil peptides, collagen, and β-sheet peptides. The design, structure, emergent properties, and applications for these multicomponent assemblies are presented in order to illustrate the potential of these formulations as sophisticated next-generation bio-inspired materials.

show abstract

Section: Peptide/biopolymer Hybridsmentioning

confidence: 99%

Multicomponent peptide assemblies

2018

View full text Add to dashboard Cite

show abstract

“…3,52,53 For example, Moyer et al 11 have shown that the location and length of the alkyl tail can drastically alter the morphology of pH-responsive, self-assembled peptide amphiphile systems, and that cylindrical nanobers had around 7-fold higher encapsulation efficiency for camptothecin compared to spherical assemblies. In contrast, Mumcuoglu et al 54 demonstrated that cell-penetrating peptide nanospheres were uptaken by the cells more compared to nanobers because peptide nanobers bound strongly to the cellular membrane and were internalized to a lesser degree by the cells. In addition, two lysine-rich peptides were shown by Newcomb et al 55 to exhibit markedly different cytotoxic effects depending on their hydrogen bonding interactions, with the H-bond-rich b-sheet forming peptide showing minimal toxicity and the H-bond-poor sequence rapidly disrupting the integrity of both cell membranes and liposomes.…”

Section: Discussionmentioning

confidence: 92%

Effects of temperature, pH and counterions on the stability of peptide amphiphile nanofiber structures

et al. 2016

Self Cite

View full text Add to dashboard Cite

Peptide amphiphiles are a class of self-assembling molecules that are widely used to form bioactive nanostructures for various applications in bionanomedicine. However, peptide molecules can exhibit distinct behaviors under different conditions, suggesting that environmental variables such as temperature, pH, electrolytes and the presence of biological factors may greatly affect the self-assembly process. In this work, we used united-atom molecular dynamics simulations to understand the effects of three counterions (Na + , Ca 2+ at pH 7 and Cl À at pH 2) and temperature change on the stability of the lauryl-VVAGERGD peptide amphiphile self-assembly. This molecule contains a bioactive RGD peptide sequence and has been shown to support cellular adhesion and proliferation in vitro. A 19-layered peptide nanostructure, containing 12 peptide amphiphile molecules per layer, was previously shown to exhibit optimal stability and it was used as the model nanofiber system. Peptide backbone stability was studied under increasing temperatures (300-358 K) using the number of hydrogen bonds and rootmean-square deviations of nanofiber size. At higher temperatures, fiber disintegration was observed to be dependent on the type of counter-ion used for nanofiber formation. Interestingly, rapid heating to higher temperatures could sometimes reestablish the integrity of the nanofiber backbone, possibly by allowing the system to bypass an energy barrier and assuming a more thermodynamically stable configuration. As counterion identity was observed to exhibit remarkable effects on the thermal stability of peptide nanofibers, we suggest that these behaviors should be considered while developing new materials for potential applications. † Electronic supplementary information (ESI) available: Observations on PA1 nanober structure under extended simulation periods, secondary structure and radius of gyration analyses of all three PA congurations, and hydrogen bond formation of PA2 nanobers. See

show abstract

“…In addition, integration of CPP to the vectors or peptide nucleic acid conjugates can be used for internaliza tion (Jung et al, 2011). Recently, CPP-decorated self-assembled peptide amphiphile (PA) nanospheres complexed with antisense oligonucleotides increased the internalization of the nanosized delivery system compared to nonbioactive PA nanostructures (Mumcuoglu et al, 2015).…”

Section: Cellular Internalization Strategiesmentioning

confidence: 99%