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Related Concept Videos

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...
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...
Roles of Electrolytes: Calcium and Phosphate01:27

Roles of Electrolytes: Calcium and Phosphate

Calcium and phosphate are essential electrolytes in the human body, with calcium being the most abundant mineral. Around 99% of the body's calcium is stored in the skeleton and teeth, forming a crystal lattice of mineral salts in combination with phosphates. Calcium plays crucial roles in various bodily functions such as blood clotting, neurotransmitter release, muscle tone maintenance, and nervous and muscle tissue excitability.
The calcium concentration in blood plasma is primarily regulated...
Essential Minerals for Bone Health01:31

Essential Minerals for Bone Health

The minerals contained in all of the food we consume are essential for our organ systems. However, certain essential minerals, such as calcium, phosphorus, magnesium, manganese, and fluoride, largely affect bone health.
Calcium and Phosphorus
Calcium is a critical component of bones, especially in the form of calcium phosphate and calcium carbonate. Since the body cannot make calcium, it must be obtained from the diet. However, calcium cannot be absorbed from the small intestine without...
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...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Related Experiment Video

Updated: Jun 8, 2026

Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis
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Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis

Published on: June 24, 2018

Phosphorylation-dependent mineral-type specificity for apatite-binding peptide sequences.

William N Addison1, Sharon J Miller, Janani Ramaswamy

  • 1Faculty of Dentistry, McGill University, Montreal, QC, Canada. william.addison@mail.mcgill.ca

Biomaterials
|October 15, 2010
PubMed
Summary

Phosphorylation significantly enhances apatite-binding peptides for bone repair biomaterials. This modification increases mineral binding and influences osteoblast mineralization, offering potential for treating pathological calcification.

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Last Updated: Jun 8, 2026

Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis
14:55

Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis

Published on: June 24, 2018

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
05:44

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Biomaterials Science
  • Biomineralization
  • Peptide Chemistry

Background:

  • Phage display identifies apatite-binding peptides for bone and tooth tissue repair.
  • Peptide phosphorylation, a crucial post-translational modification, is absent in current display peptides, limiting biomaterial design.
  • Understanding peptide-mineral interactions is key to developing effective biomaterials.

Purpose of the Study:

  • To investigate the effects of phosphorylation and sequence scrambling on peptide adsorption to various apatites.
  • To determine critical design parameters (net charge, charge distribution, sequence, composition) controlling peptide affinity for bone-like mineral.
  • To assess the impact of modified peptides on osteoblast mineralization and their potential in managing pathologic calcification.

Main Methods:

  • Investigated peptide adsorption to four apatite types (bone-like, hydroxyapatite with varying carbonate content).
  • Utilized phosphorylation and sequence scrambling of the VTKHLNQISQSY (VTK) peptide.
  • Assessed osteoblast culture mineralization and employed computational modeling for peptide-mineral interactions.

Main Results:

  • Phosphorylation increased VTK peptide adsorption 10-fold to bone-like mineral and 2-fold to carbonated apatite; no effect on pure hydroxyapatite.
  • Sequence scrambling enhanced nonphosphorylated VTK peptide specificity for bone-like mineral.
  • Phosphorylated VTK peptide (pVTK) dose-dependently inhibited osteoblast mineralization, unlike nonphosphorylated forms.

Conclusions:

  • Phosphorylation of serine residues enhances peptide specificity for bone-like mineral, primarily driven by composition and net charge.
  • Sequence order, alongside net charge, modulates osteoblast mineralization, with pVTK showing inhibitory effects.
  • These peptides, particularly phosphorylated variants, show potential for managing pathological calcification.