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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Ligand Binding Sites02:40

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Drug Distribution: Tissue Binding01:21

Drug Distribution: Tissue Binding

Upon entering the systemic circulation, drugs can distribute into the interstitial and intracellular fluid of various tissue cells. This distribution is facilitated by the binding of drugs to different cellular components within tissues, which may lead to drug accumulation in specific areas. Drugs bound to tissue components serve as reservoirs that release free drugs back into the system, prolonging the drug's overall action. However, this accumulation can also result in local toxicity.
For...

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Engineering Antiviral Agents via Surface Plasmon Resonance
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Published on: June 14, 2022

Surface-bound proteins with preserved functionality.

Jiandi Wan1, Marlon S Thomas, Sean Guthrie

  • 1Department of Bioengineering, University of California, Riverside, A-220 Bourns Hall, Riverside, CA 92521, USA.

Annals of Biomedical Engineering
|March 25, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed a method to attach proteins to surfaces using polyethylene glycol (PEG) layers. This creates bioactive interfaces that resist unwanted interactions, crucial for medical and biological applications.

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Area of Science:

  • Materials Science
  • Surface Chemistry
  • Biotechnology

Background:

  • Material biocompatibility is dictated by surface properties.
  • Controllable surface modification is key for advanced chemical, biological, and medical applications.
  • Bioactive interfaces must exhibit designed activity while preventing nonspecific interactions.

Purpose of the Study:

  • To describe a method for chemically modifying glass and silicon surfaces with protein-functionalized polyethylene glycol (PEG) layers.
  • To create surfaces that are both bioactive and resistant to nonspecific binding.
  • To investigate the covalent attachment of proteins to aldehyde-functionalized PEG layers.

Main Methods:

  • Coating substrates with acetals (protected aldehydes) to form aldehyde-functionalized surfaces.
  • Using a mild Lewis acid for aldehyde deprotection, avoiding surface degradation.
  • Introducing alpha,omega-bifunctional polymers for covalent attachment of proteins like green fluorescent protein and bovine carbonic anhydrase.

Main Results:

  • Successful covalent attachment of proteins to PEG-modified surfaces.
  • Spectroscopic evidence confirmed that surface-bound proteins retained their functionalities.
  • Protein surface concentrations did not linearly correlate with the molar fractions of bifunctional PEGs used, indicating complex surface loading.

Conclusions:

  • The developed procedure enables the creation of functionalized surfaces with controlled protein immobilization.
  • The findings highlight that predicting surface protein loading based on reagent solution composition is not straightforward.
  • This method offers a pathway for designing advanced bioactive interfaces for diverse applications.