Related Experiment Video
Updated: Feb 13, 2026
10:01
Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
6.4K
Protein delivery into cells using inorganic nanoparticle-protein supramolecular assemblies
Federica Scaletti1, Joseph Hardie, Yi-Wei Lee
1Department of Chemistry, University of Massachusetts Amherst, 710 N. Pleasant St., Amherst, USA. rotello@chem.umass.edu.
Chemical Society Reviews
|March 15, 2018
Summary
This review explores novel nanoassemblies for therapeutic protein delivery, focusing on strategies and challenges for effective intracellular protein delivery to treat diseases.
Area of Science:
- Biotechnology
- Nanomedicine
- Cellular Biology
Background:
- Protein delivery into cells holds significant therapeutic potential for various diseases.
- Current methods face challenges in achieving efficient intracellular delivery.
Purpose of the Study:
- To review recent advancements in nanoassembly strategies for protein delivery.
- To discuss factors influencing the efficacy of nanoparticle-based protein delivery.
- To highlight challenges in achieving cytosolic protein delivery.
Main Methods:
- Review of recently developed nanoassembly strategies (direct assembly, encapsulation, composite formation).
- Analysis of factors affecting nanoassembly efficacy from nanoparticle and protein perspectives.
- Discussion of endosomal escape and evasion mechanisms for cytosolic delivery.
Main Results:
- Nanoassemblies offer diverse strategies for protein delivery.
- Efficacy is influenced by nanoparticle characteristics and protein properties.
- Endosomal escape remains a critical hurdle for successful cytosolic delivery.
Conclusions:
- Nanoassemblies represent a promising frontier for therapeutic protein delivery.
- Overcoming endosomal barriers is key to unlocking the full potential of intracellular protein therapeutics.
- Further research is needed to optimize nanoassembly design for enhanced therapeutic outcomes.
Related Concept Videos
02:41Protein Complex Assembly
16.9K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.9K
02:41Protein Complex Assembly
2.6K
2.6K
02:15Protein and Protein Structure
88.9K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
88.9K
02:04Protein-protein Interfaces
14.8K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.8K
03:06From DNA to Protein
22.6K
The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
22.6K
02:26Conservation of Protein Domains Over Different Proteins
14.7K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.7K