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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Asymmetric Lipid Bilayer01:35

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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
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Lipids as Anchors01:32

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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Drug Binding to Blood Components

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When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
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Updated: Dec 29, 2025

Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
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Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A.

Nicholas M Frame1, Meera Kumanan2, Thomas E Wales3

  • 1Department of Physiology & Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA, 02118, United States.

Journal of Molecular Biology
|February 10, 2020
PubMed
Summary

Serum amyloid A (SAA) protein

Keywords:
hydrogen-deuterium exchange mass spectrometryinflammation and immunitylipoprotein nanoparticlemolecular dynamics simulationsβ-hairpin misfolding intermediate

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Serum amyloid A (SAA) is a crucial plasma protein involved in lipid transport during inflammatory responses.
  • Understanding SAA's structure and function is vital for comprehending lipid metabolism and inflammatory diseases.

Purpose of the Study:

  • To elucidate the solution conformations of SAA.
  • To investigate the mechanism of lipid binding by SAA.
  • To explore the structural basis of SAA's role in inflammation and amyloid formation.

Main Methods:

  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS)
  • Lipoprotein reconstitution assays
  • Amino acid sequence analysis
  • Molecular dynamics (MD) simulations

Main Results:

  • SAA's solution conformations closely resemble crystal structures, with notable differences.
  • A lipid-binding site, formed by α-helices h1 and h3, is pre-formed in solution and stabilized by lipid binding.
  • Lipid binding induces folding of helix h3, creating a concave hydrophobic surface for apolar ligand sequestration.
  • The C-terminal region is dynamic and likely mediates binding to other ligands.
  • A β-hairpin in the h1-h2 linker may represent an early amyloidogenic intermediate.

Conclusions:

  • SAA possesses a pre-formed, adaptable lipid-binding site crucial for its function.
  • Structural insights into SAA's lipid interactions, ligand binding, and amyloidogenic potential are established.
  • This study provides a foundation for understanding SAA's role in health and disease, including amyloidosis.