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Penetratin-induced Aggregation and Subsequent Dissociation of Negatively Charged Phospholipid Vesicles

Daniel Persson (Institutionen för fysikalisk kemi) ; Per Thorén (Institutionen för fysikalisk kemi) ; Bengt Nordén (Institutionen för fysikalisk kemi)
FEBS Letters (0014-5793 ). Vol. 505 (2001), 2, p. 307-312.
[Artikel, refereegranskad vetenskaplig]

The interaction of the cellular delivery vector penetratin with a model system consisting of negatively charged phospholipid vesicles has been studied. Above a certain peptide to lipid molar ratio, the cationic oligopeptide induces vesicle aggregation. Interestingly, the aggregation is followed by spontaneous disaggregation, which may be related to membrane translocation of the peptide. Circular dichroism (CD) measurements indicate a conformational transition, from alpha -helix to antiparallel beta -pleated sheet, which is simultaneous with the aggregation process. The potential influence of spectroscopic artifacts on CD data due to the drastically increased turbidity during aggregation is discussed.

Nyckelord: Antennapedia homeodomain, penetratin, vesicle aggregation, circular dichroism, artifact; turbidity



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Denna post skapades 2011-01-05. Senast ändrad 2011-07-01.
CPL Pubid: 132479

 

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Institutioner (Chalmers)

Institutionen för fysikalisk kemi (1900-2003)

Ämnesområden

Energi
Livsvetenskaper
Materialvetenskap
Nanovetenskap och nanoteknik
Fysikalisk kemi

Chalmers infrastruktur