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Related Concept Videos

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphodiester Linkages01:01

Phosphodiester Linkages

Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...

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Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles (PPAs) and Related Biomaterials
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Tailoring cyclic polyamines for inorganic/organic phosphate binding.

Carla Bazzicalupi1, Andrea Bencini, Vito Lippolis

  • 1Dipartimento di Chimica Ugo Schiff, Polo Scientifico, Università degli Studi di Firenze, Via della Lastruccia 3, 50019 Sesto Fiorentino, Firenze, Italy.

Chemical Society Reviews
|September 8, 2010
PubMed
Summary

This review covers metal-free cyclic receptors designed for binding phosphate guests in water. We explore structural evolution optimizing non-covalent interactions for enhanced phosphate recognition.

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Area of Science:

  • Supramolecular Chemistry
  • Organic Chemistry
  • Chemical Biology

Background:

  • Phosphate recognition is crucial in biological systems.
  • Designing synthetic receptors for phosphate binding in aqueous environments presents challenges.
  • Metal-free hosts offer an alternative to traditional metal-based complexation.

Purpose of the Study:

  • To review significant achievements in structure-based design of cyclic receptors for phosphate guests.
  • To highlight the evolution of these receptors for optimal binding via non-covalent interactions.
  • To focus on receptors with aliphatic amine groups acting as metal-free hosts in aqueous media.

Main Methods:

  • Structure-based design principles.
  • Synthesis of cyclic receptors with aliphatic amine functionalities.
  • Investigation of non-covalent interactions (e.g., hydrogen bonding, electrostatic interactions).
  • Binding studies of inorganic phosphates and mononucleotide anions in aqueous solutions.

Main Results:

  • Demonstration of successful structure-based design leading to effective phosphate binding.
  • Evolutionary pathways showing improved receptor architectures and binding affinities.
  • Identification of key structural factors and non-covalent interactions governing phosphate recognition.
  • Examples of receptors binding diverse phosphate species, including inorganic phosphates and nucleotide anions.

Conclusions:

  • Cyclic receptors with aliphatic amines are effective metal-free hosts for phosphates in water.
  • Structure-based design and optimization of non-covalent interactions are key to high-affinity phosphate binding.
  • These synthetic receptors show promise for applications in sensing, separation, and biological studies involving phosphates.