Studies on the aggregation and possible channel formation in membranes of a cyclic hexapeptide, cyclo (D-Ala-L-Pro-L-Ala)2.
The interaction of zwitterionic lipid DMPC and DPPC with cyclic hexapeptide, cyclo (D-Ala-L-Pro-L-Ala)2 was studied using circular dichroism (CD) and differential scanning calorimetry (DSC). Preliminary membrane conductance results showed that the peptide has a tendency to form channels inside the lipid bilayer. CD studies indicated that as the lipid/peptide (L/P) ratio (DMPC/peptide) was increased, the magnitude of the negative CD band having a lambda(max) around 200 nm decreased. At a L/P ratio of 210:1, this band disappeared completely, indicating dramatic conformational changes in the peptide on interaction with the lipid bilayer. Reduction of the phase transition temperature and the maximum heat capacity of the lipid bilayer (DPPC) for gel-to-liquid crystalline phase transition indicates a strong interaction of the peptide with the lipid bilayer.
Ramesh
J
J
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Ghosh
J K
JK
Swaminathan
C P
CP
Ramasamy
P
P
Surolia
A
A
Sikdar
S K
SK
Easwaran
K R K
KR
D001692:Biological Transport; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003500:Cyclization; D004553:Electric Conductivity; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D013696:Temperature
D008051:Lipid Bilayers; D008565:Membrane Proteins; D010455:Peptides