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Protein Complex Assembly02:41

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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.
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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...
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Cucurbituril-Based Biomacromolecular Assemblies.

Yao-Hua Liu1, Ying-Ming Zhang1, Hua-Jiang Yu1

  • 1College of Chemistry, State Key Laboratory of Elemento-Organic Chemistry, Nankai University, Tianjin, 300071, China.

Angewandte Chemie (International Ed. in English)
|August 29, 2020
PubMed
Summary
This summary is machine-generated.

Cucurbiturils (CBs) are macrocyclic receptors enabling advanced biomacromolecular assemblies. These versatile structures show promise in biosensing, disease treatment, and subcellular bioimaging applications.

Keywords:
bioimagingcucurbiturilsnucleic acidspeptidesproteins

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Area of Science:

  • Supramolecular Chemistry
  • Biomacromolecular Assemblies

Background:

  • Cucurbiturils (CBs) are macrocyclic receptors with unique structural features like hydrophobic cavities and carbonyl portals.
  • CBs exhibit advantageous molecular recognition properties for biomacromolecules such as peptides, nucleic acids, and proteins.

Purpose of the Study:

  • This minireview highlights recent advancements in CB-based biomacromolecular assemblies.
  • Focuses on the diverse applications of these assemblies in various scientific and medical fields.

Main Methods:

  • Review of existing literature on cucurbituril-based supramolecular chemistry.
  • Analysis of case studies demonstrating CB applications.

Main Results:

  • CB-based assemblies are effective in biosensors and assays.
  • CBs facilitate the regulation of biochemical reactions.
  • CBs show potential in treating diseases and in subcellular bioimaging.

Conclusions:

  • CB-based supramolecular architectures offer numerous applications from fundamental research to translational medicine.
  • The versatility of CBs makes them valuable tools in diverse scientific disciplines.