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Protein Complex Assembly

Protein Complex Assembly

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...

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Coat Assembly and GTPases

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Assembly of Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Related Experiment Video

Updated: Jul 12, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Enzyme-Instructed Intracellular Peptide Assemblies.

Zhiyu Liu¹, Jiaqi Guo¹, Yuchen Qiao¹

¹Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02453, United States.

Accounts of Chemical Research

|October 26, 2023

Summary

This summary is machine-generated.

Enzyme-instructed self-assembly (EISA) creates intracellular peptide assemblies for novel biomedicines, including cancer nanomedicines and cell morphogenesis control. This approach offers precise targeting of cellular components with high selectivity.

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

Biomedical Engineering
Supramolecular Chemistry
Nanomedicine

Background:

Supramolecular assemblies are vital for cellular functions and inspire synthetic biomimetic therapeutics.
Peptide assemblies, particularly those formed via enzyme reactions, are rapidly advancing as a novel therapeutic class.

Purpose of the Study:

To review the application of enzyme-instructed self-assembly (EISA) for generating intracellular peptide assemblies.
To highlight EISA's potential in developing novel cancer nanomedicines and controlling cell morphogenesis.

Main Methods:

Enzyme-instructed self-assembly (EISA) to create intracellular peptide assemblies.
Targeting of subcellular organelles (mitochondria, ER, Golgi, lysosomes, nucleus) using EISA-formed assemblies.
Exploration of transcytosis for controlling cell morphogenesis.

Main Results:

EISA enables localized, non-diffusive peptide assembly formation within cells.
Demonstrated selective targeting of various subcellular organelles for potential cancer therapeutics.
Showcased EISA's role in modulating cell morphogenesis through transcytosis.

Conclusions:

EISA is a versatile and cell-compatible approach for creating targeted intracellular peptide assemblies.
EISA-generated assemblies hold significant promise for disease understanding, cell behavior control, and novel therapeutic development.
This approach leverages enzyme substrates as building blocks for advanced self-assembly in biomedicine.