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Liposomal cargo unloading induced by pH-sensitive peptides.

H-M Lee1, J Chmielewski

  • 1Department of Chemistry, Purdue University, West Lafayette, IN 47906, USA.

The Journal of Peptide Research : Official Journal of the American Peptide Society
|March 25, 2005
PubMed
Summary

Researchers developed pH-sensitive peptides that change shape and disrupt membranes at acidic endosomal pH. This design enables targeted release of liposomal contents, showing successful control over membrane activity.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Drug Delivery

Background:

  • Amphiphilic peptides are crucial for membrane interactions.
  • Controlling peptide conformation based on pH is key for targeted drug delivery.
  • Endosomal pH is significantly lower than physiological pH.

Purpose of the Study:

  • To design and investigate peptides with pH-dependent conformational changes.
  • To achieve membrane disruption and content release at endosomal pH.
  • To optimize peptide sequences for lipid binding and pH responsiveness.

Main Methods:

  • Peptide synthesis incorporating glutamic acid (Glu) and leucine (Leu) residues.
  • Circular dichroism (CD) spectroscopy in aqueous and liposomal environments.
  • Liposomal content release assays at neutral and acidic pH.

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Main Results:

  • Peptides exhibited a random coil conformation at physiological pH.
  • Acidification induced a switch to amphiphilic alpha-helical structures.
  • Significant liposomal content release was observed at acidic pH, confirming design efficacy.

Conclusions:

  • The designed peptides demonstrate effective pH-dependent conformational switching.
  • This strategy enables targeted membrane disruption and cargo release at endosomal pH.
  • The study validates the use of Glu and Leu residues for pH-responsive, membrane-active peptides.