Diffusion and dynamics of penetratin in different membrane mimicking media

August Andersson, Jonas Almqvist, Franz Hagn, Lena Mäler

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

Abstract

The interaction between the cell-penetrating peptide (CPP) penetratin and different membrane mimetic environments has been investigated by two different NMR methods: 15N spin relaxation and translational diffusion. Diffusion coefficients were measured for penetratin in neutral and in negatively charged bicelles of different size, in sodium dodecyl sulfate micelles (SDS), and in aqueous solution. The diffusion coefficients were used to estimate the amount of free and bicelle/micelle-bound penetratin and the results revealed that penetratin binds almost fully to all studied membrane mimetics. 15N relaxation data for three sites in penetratin were interpreted with the model-free approach to obtain overall and local dynamics. Overall correlation times for penetratin were in agreement with findings for other peptides of similar size in the same solvents. Large differences in order parameters were observed for penetratin in the different membrane mimetics. Negatively charged surfaces were seen to restrict motional flexibility, while a more neutral membrane mimetic did not. This indicates that although the peptide binds to both bicelles and SDS micelles, the interaction between penetratin and the various membrane mimetics is different.

Original languageEnglish
Pages (from-to)18-25
Number of pages8
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1661
Issue number1
DOIs
StatePublished - 10 Feb 2004
Externally publishedYes

Keywords

  • Bicelle
  • Diffusion
  • Dynamics
  • N relaxation
  • NMR
  • PFG
  • Penetratin

Fingerprint

Dive into the research topics of 'Diffusion and dynamics of penetratin in different membrane mimicking media'. Together they form a unique fingerprint.

Cite this