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Covalent Bonds01:29

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When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
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Compared to ionic bonds, which results from the transfer of electrons between metallic and nonmetallic atoms, covalent bonds result from the mutual attraction of atoms for a “shared” pair of electrons.
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Updated: Jan 29, 2026

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Folate-Functionalized Albumin-Containing Systems: Non-Covalent vs. Covalent Binding of Folic Acid.

Maria G Gorobets1, Anna V Toroptseva1, Madina I Abdullina1

  • 1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 4, Kosygina Street., Moscow 119334, Russia.

Pharmaceutics
|January 28, 2026
PubMed
Summary
This summary is machine-generated.

Folate-modified albumin nanoparticles enhance cancer and inflammatory disease treatments. This review details folate-albumin binding, nanoparticle function, and stability for improved medical targeting.

Keywords:
NHS-esteralbumincarbodiimide reactionconjugationcovalent bindingfolate-albumin conjugationfolic acidnano- and submicron particles (NSPs)non-covalent binding

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Drug Delivery

Background:

  • Nano- and submicron particles (NSPs) functionalized with folate are key for cancer and inflammatory disease diagnosis and treatment.
  • Albumin-based systems offer improved biocompatibility, circulation time, and colloidal stability for medical applications.
  • Albumin's binding capacity facilitates the transport of therapeutic and imaging agents.

Purpose of the Study:

  • To review the binding of folic acid to NSPs and the subsequent function of folate-albumin-NSPs.
  • To analyze the types of bonds (covalent and non-covalent) between folic acid and albumin.
  • To examine the impact of binding conditions on the characteristics and function of the resulting folate-albumin-NSPs.

Main Methods:

  • Physicochemical methods for confirmation and quantification of folate-albumin binding.
  • Analysis of reaction conditions influencing binding processes.
  • Investigation of serum albumin structure modification during folate binding, including involved amino acid residues and conformational changes.

Main Results:

  • Detailed examination of covalent and non-covalent binding between folic acid and albumin.
  • Characterization of binding processes, product properties, and functional outcomes under various conditions.
  • Assessment of albumin's structural state and stability within folate-albumin-NSPs.
  • Evaluation of targeting effectiveness as influenced by folate-albumin binding characteristics.

Conclusions:

  • Folate-albumin-NSPs show promise for targeted therapies, with binding characteristics crucial for efficacy.
  • Understanding albumin's structural and conformational changes is vital for optimizing NSP function.
  • Addressing existing challenges in creating folate-modified albumin-NSPs can lead to improved therapeutic and diagnostic tools.