Coordination Chemistry in Protein Cages: Principles, Design, and Applications
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Problem URL. Describe the connection issue. SearchWorks Catalog Stanford Libraries. Coordination chemistry in protein cages : principles, design, and applications.
Molecular Metal Oxides in Protein Cages/Cavities
Responsibility edited by Takafumi Ueno, Yoshihito Watanabe. Online Available online. More options. Find it at other libraries via WorldCat Limited preview.
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This mechanism can be applied to deliver drugs to acidic cancer microenvironments. The disassembly and reassembly of the protein cages based on environmental conditions could also aid drug loading and release. The release mechanism of loaded molecules could be tuned by introducing repulsive forces at the intersubunit interfaces to facilitate environment e. Nanoparticles accumulate in the cancer microenvironment by enhanced permeation and retention EPR effect due to the leaky vasculature of the tissue. Nonspecific accumulation through the enhanced permeation and retention effect is referred to as passive targeting and may not be very effective.
To enhance the affinity for target cells, the carriers can be decorated with targeting ligands to impart active targeting. Targeted delivery of drugs by carrier systems can reduce the amount of drug-carrier complex needed for therapy. An example of active targeting ligand is the peptide RGD, which is present in adenoviruses and has a natural affinity for upregulated integrin receptors in endothelial cells of tumor vessels. Attaching this peptide to the external surface of a carrier aids tumor-targeted delivery.
Certain tumor delivery platforms focus on targeting the surface receptors using natural ligands that facilitate endocytosis, 44 such as folate receptors in cancer cells, transferrin receptors and epidermal growth factor receptors. One of the emerging areas of interest is the modulation of the immune response using protein carriers for application in tumor immunotherapy and the treatment of autoimmune diseases. Non-natural peptide ligands are often identified using phage-display libraries that provide the opportunity to screen multiple ligands with different affinities towards a specific cell receptor.
Aptamers are nucleotide-based molecules that have been garnering interest as targeting ligands.
The targeting ability of a carrier depends mainly on its surface ligand density, which can be tuned on protein nanocages to suit a given application. Similar to other nanoparticles, the application of protein nanocages in biomedicine involves several challenges: 1 lack of a natural capability to carry drugs, 2 lack of specificity, 3 low cell uptake efficiency, 4 absence of endosomal escape mechanism, 5 limited circulation time, 6 potential to trigger an immunological response and 7 lack of tuneable release properties. For example, the translocation of these carriers into cells through endocytosis is not always advantageous as these materials are digested in the lysosome rather than shuttled into the target cell organelle.
Hence, incorporating an endosomal escape mechanism into protein nanocages is beneficial. What distinguishes nanocage-based delivery systems from other inorganic nanoparticles is the spatial control of functional groups and the ligands attached to the protein structure. Multifunctional properties can be achieved by combining the desired modifications for loading, targeting and chimeric assembly, leading to the development of smart nanocarriers with tremendous potential in nanomedicine. The structure of protein nanocages offers three distinct surfaces for engineering: the interior, exterior and intersubunit interface Figure Protein cage modifications at distinct interfaces 64 reprinted from Uchida, M.
Acta 8 , — The interior cavity of the protein nanocages provides an ideal containment for molecular cargos. Tailoring the cage interior increases the encapsulation efficiency, binding affinity and modulated release profile.
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Genetic or chemical alterations can be made at precise locations to manipulate the nucleation and attachment of molecules. Antibodies are potential cargo for larger protein nanocages, such as vaults. Modification of the nanocage interior by introducing cysteine residues has been a widely used approach. The modification facilitates covalent attachment of dye molecules, drugs and other active molecules through disulfide bonds.
Abedin et al. The polymer network was created by the sequential conjugation of multifunctional monomeric units by click chemistry, allowing the free amines to be incorporated into the polymer for internal functionalization Figure Design of protein nanocage-polymer hybrids. Synthesis of a cross-linked branched polymer network in the interior of a protein cage.
The exterior surface of protein nanocages is engineered to impart increased circulatory half-life, local accumulation, cellular penetration and triggering of specific cellular responses. The unique geometry of protein nanocages allows for multiple ligands and functional molecules to be displayed on their surfaces. Modifying molecules include small molecules e.
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RGD, transactivator of transcription 47—57 peptide cell penetrating peptide , immunoglobulin G binding peptide Z domain , antibodies e. The exterior surfaces of CPMV, cowpea chlorotic mottle virus CCMV and bacteriophages M13, Qb and MS2 have been modified with antibodies, peptides, transferrin and cell transduction domains or cell-penetrating peptides. Modification of protein carriers with this peptide has been proven to aid tumor targeting.
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These aptamers can bind to both extracellular membrane and intracellular proteins, thus facilitating aptamer—nanoparticle conjugate therapy. PEG and enhance penetration into cells e. Folate-PEG displayed on adenoviral nanoparticles has been delivered to folate receptor-overexpressing cells. These nanocarriers were proven to decrease the interleukin-6 levels of macrophages, showing that the engineered viral scaffolds counteract the innate immune response.
The spatial control of multifunctional groups on protein nanocages equips them for both hierarchical self-assembly and display of distinct functional ligands. Display of multiple types of ligands in a precise arrangement on nanoparticles is challenging.
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A distinct advantage of protein nanocages over other nanoparticles is that the position of each amino acid is spatially defined, allowing for precise spatial control of the displayed ligands. The N or C termini of the nanocage subunits that face the external surface are a natural choice for displaying functional ligands. Fusion of short peptides to these termini has been achieved through genetic engineering.
The display of two types of HIV-derived antigenic epitopes pep23 and RT2 provokes specific antibodies and T-cell responses.