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Related Concept Videos

Antifungal Agents01:15

Antifungal Agents

62
Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to...
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Pore Transport and Ion-Pair Transport01:17

Pore Transport and Ion-Pair Transport

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Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited  but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
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Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Drug Elimination by Renal Route: Tubular Secretion01:15

Drug Elimination by Renal Route: Tubular Secretion

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Once the process of glomerular filtration is completed, blood carrying unfiltered drug molecules traverses through efferent arterioles and makes its way into the peritubular capillaries in the proximal tubule. A variety of carriers play a pivotal role in actively secreting drugs from these peritubular capillaries into the tubular fluid. The organic anion transporter transfers acidic drugs, against an electrochemical gradient, from the peritubular capillaries into the renal tubule cells and...
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Related Experiment Video

Updated: Apr 4, 2026

Preparation and Utilization of Freshly Isolated Human Detrusor Smooth Muscle Cells for Characterization of 9-Phenanthrol-Sensitive Cation Currents
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Taming Amphotericin B.

Vaclav Janout1, Wiley A Schell2, Damien Thévenin1

  • 1Department of Chemistry, Lehigh University , Bethlehem, Pennsylvania 18015, United States.

Bioconjugate Chemistry
|September 5, 2015
PubMed
Summary
This summary is machine-generated.

A novel molecular umbrella strategy significantly reduces the toxicity of Amphotericin B, a potent antifungal drug. This approach enhances cellular selectivity while maintaining antifungal efficacy, offering a safer therapeutic option.

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Area of Science:

  • Medicinal Chemistry
  • Drug Delivery
  • Antifungal Research

Background:

  • Amphotericin B (AmB) is a vital antifungal agent but suffers from significant toxicity.
  • High toxicity limits Amphotericin B's clinical application, necessitating strategies for improved selectivity.
  • Membrane-disrupting agents often exhibit dose-limiting side effects due to non-specific interactions.

Purpose of the Study:

  • To develop a strategy for enhancing the cellular selectivity of membrane-disrupting agents like Amphotericin B.
  • To create a novel conjugate of Amphotericin B with a molecular umbrella to mitigate toxicity.
  • To evaluate the antifungal activity, hemolytic activity, and cytotoxicity of the new conjugate.

Main Methods:

  • A molecular umbrella construct was designed using spermidine and cholic acid derivatives.
  • Amphotericin B was chemically coupled to the molecular umbrella.
  • Antifungal activity, hemolytic activity against red blood cells, and cytotoxicity against HEK293 T cells were assessed.

Main Results:

  • The Amphotericin B-molecular umbrella conjugate demonstrated potent antifungal activity comparable to native Amphotericin B.
  • Hemolytic activity of the conjugate was dramatically reduced compared to Amphotericin B.
  • Cytotoxicity of the conjugate towards HEK293 T cells was significantly diminished.

Conclusions:

  • The molecular umbrella strategy effectively enhances the cellular selectivity of Amphotericin B.
  • This approach offers a promising method to reduce the toxicity of membrane-disrupting antifungal agents.
  • The developed conjugate represents a potentially safer therapeutic alternative for fungal infections.