Cooperative DNA binding and assembly by a bZip peptide-amphiphile

Tu, Raymond S.; Marullo, Rachel; Pynn, R.; Bitton, Ronit; Bianco‐Peled, Havazelet; Tirrell, Matthew

doi:10.1039/b922295b

Cited by 26 publications

(37 citation statements)

References 73 publications

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“…Interestingly, confining and crowding the peptide within the micelle corona gives an artificial tertiary structure that facilitates J8 peptide becoming highly α-helical (42.5%, Fig. 1d), which agrees with previous research that has shown the capacity of peptide amphiphile micelles to reestablish native peptide secondary structure (50)(51)(52). Annealing the micelles induced them to form much longer structures (Fig.…”

Section: Discussionsupporting

confidence: 79%

Peptide Amphiphile Micelles Self-Adjuvant Group A Streptococcal Vaccination

Trent

Ulery

Black

et al. 2014

AAPS J

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Abstract. Delivery system design and adjuvant development are crucially important areas of research for improving vaccines. Peptide amphiphile micelles are a class of biomaterials that have the unique potential to function as both vaccine delivery vehicles and self-adjuvants. In this study, peptide amphiphiles comprised of a group A streptococcus B cell antigen (J8) and a dialkyl hydrophobic moiety (diC 16 ) were synthesized and organized into self-assembled micelles, driven by hydrophobic interactions among the alkyl tails. J8-diC 16 formed cylindrical micelles with highly α-helical peptide presented on their surfaces. Both the micelle length and secondary structure were shown to be enhanced by annealing. When injected into mice, J8-diC 16 micelles induced a strong IgG1 antibody response that was comparable to soluble J8 peptide supplemented with two classical adjuvants. It was discovered that micelle adjuvanticity requires the antigen be a part of the micelle since separation of J8 and the micelle was insufficient to induce an immune response. Additionally, the diC 16 tail appears to be non-immunogenic since it does not stimulate a pathogen recognition receptor whose agonist (Pam 3 Cys) possesses a very similar chemical structure. The research presented in this paper demonstrates the promise peptide amphiphile micelles have in improving the field of vaccine engineering.

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Section: Discussionsupporting

confidence: 79%

Peptide Amphiphile Micelles Self-Adjuvant Group A Streptococcal Vaccination

Trent

Ulery

Black

et al. 2014

AAPS J

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“…Small peptide sequences isolated from parent proteins generally lose their secondary structure, which can be detrimental to their activity 25–26 . As observed with bZip, the peptide loses its native secondary structure but regains some degree of helical content after lipid conjugation, and exhibits greatly enhanced folding in the headgroup of micelles 5,27 . Interestingly, circular dichroism (CD) of di-C 16 -bZip showed that the PAs within the PRTNs possessed enhanced α-helical content, resembling that of micelles, with minima at 208 nm and 222 nm (Fig.…”

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confidence: 72%

“…The binding of the bZip PRTNs to long calf-thymus DNA (ctDNA) strands was studied to supplement the anisotropy experiments. Previous work showed that bZip micelles rearranged to form lamellar sheets upon complexation with ctDNA 5 , whereas atomic force microscopy (AFM) shows that the bZip PRTNs maintained their integrity upon complexation (Fig. 3d–f).…”

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confidence: 89%

“…The critical aggregation concentration determined with the pyrene fluorescence method 23 revealed that the value for the di-C 16 -NLS PAs was 60.4 μM, whereas the CAC of the PRTNs was an order of magnitude lower at 5.6 μM (see Supplemental Information). Due to the low CAC of di-C 16 -bZip micelles 5 , an alternate method had to be employed to determine their stability. The dissociation kinetics of fluorescein labeled di-C 16 -bZip micelles and PRTNs in the presence of bovine serum albumin were measured using fluorescence quenching experiments 24 .…”

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confidence: 99%

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De Novo Design of Bioactive Protein-Resembling Nanospheres via Dendrimer-Templated Peptide Amphiphile Assembly

et al. 2011

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Self-assembling peptide amphiphiles (PAs) have been extensively used in the development of novel biomaterials. Due to their propensity to form cylindrical micelles, their use is limited in applications where small spherical micelles are desired. Here we present a platform method for controlling the self-assembly of biofunctional PAs into spherical 50 nm particles using dendrimers as shape-directing scaffolds. This templating approach results in biocompatible, stable protein-like assemblies displaying peptides with native secondary structure and biofunctionality.

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“…In order for such practical applications to further advance the precise understanding of surface engineering principles, stability of assembled structures, biodistribution, and the cell-material interface created by peptide-based materials and living systems will be very important. Two key aspects of PAs' capabilities to control biological systems will be to control protein and nucleic acid function within and outside the cell 103,166,[189][190][191][192][193][194] and to three-dimensionally mimic the naturally occurring extracellular matrices 7,11,73,115,118,[195][196][197] if these two functions are combined and well defined, then some of the undefined components pertaining to biomedical applications, such as stem cell tissue engineering and targeted drug delivery, can incorporate more quantitative subcomponents. …”

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confidence: 99%