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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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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...
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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...
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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.

Roberta Piacentini1, Alberto Boffi2, Edoardo Milanetti1,3

  • 1Department of Physics, University "Sapienza", Piazzale Aldo Moro 5, 00185 Rome, Italy.

Pharmaceuticals (Basel, Switzerland)
|March 28, 2024
PubMed
Summary

Lactoferrins and their peptides boost innate immunity with antimicrobial and anti-inflammatory effects. Understanding their structural interactions is key to developing new pharmaceutical products.

Keywords:
antimicrobial activityantiviral activitylactoferrinlactoferrin-derived peptidesmechanism of action

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Area of Science:

  • Biochemistry and Molecular Biology
  • Immunology
  • Pharmacology

Background:

  • Lactoferrins and derived peptides possess diverse innate immune functions, including antimicrobial, anti-inflammatory, immunomodulatory, and antitumor activities.
  • The precise molecular mechanisms underlying lactoferrin interactions with targets are not fully elucidated.
  • Advancements in in silico methods are enabling large-scale investigations into these macromolecular interactions.

Purpose of the Study:

  • To review the current understanding of structural determinants governing lactoferrin recognition of molecular targets.
  • To focus on the mechanisms of lactoferrin activity against bacterial and viral pathogens.
  • To highlight the importance of structural insights for developing novel pharmaceutical products.

Main Methods:

  • Literature review focusing on structural biology and computational methods.
  • Analysis of existing studies on lactoferrin-target interactions.
  • Synthesis of knowledge regarding mechanisms of action against microbes.

Main Results:

  • Lactoferrin's biological actions are diverse, with varied proposed mechanisms.
  • Structural insights into lactoferrin-target binding are limited but expanding.
  • In silico approaches are crucial for large-scale investigation of these interactions.

Conclusions:

  • Understanding the structural basis of lactoferrin-target interactions is critical.
  • This knowledge is essential for the rational design of new pharmaceutical agents.
  • Further research into lactoferrin's structural determinants will advance innate immunity therapeutics.