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Interaction of dipalmitoyl phosphatidylcholine (DPPC) liposomes and insulin
Authors:Mohsen M. Mady  Wael M. Elshemey
Affiliation:1. Faculty of Science, Biophysics Department , Cairo University , Giza 12613, Egypt;2. Department of Physics and Astronomy, College of Science , King Saud University , Riyadh-11451, Saudi Arabia dr_mmady@yahoo.com;4. Faculty of Science, Biophysics Department , Cairo University , Giza 12613, Egypt
Abstract:Insulin, a peptide that has been used for decades in the treatment of diabetes, has well-defined properties and delivery requirements. Liposomes, which are lipid bilayer vesicles, have gained increasing attention as drug carriers which reduce the toxicity and increase the pharmacological activity of various drugs. The molecular interaction between (uncharged lipid) dipalmitoyl phosphatidylcholine (DPPC) liposomes and insulin has been characterized by using Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction. The characteristic protein absorption band peaks, Amide I (at about 1660?cm?1) and Amide II band (at about 1546?cm?1) are potentially reduced in the liposome insulin complex. Wide-angle x-ray scattering measurements showed that the association of insulin with DPPC lipid of liposomes still maintains the characteristic DPPC diffraction peaks with almost no change in relative intensities or change in peak positions. The absence of any shift in protein peak positions after insulin being associated with DPPC liposomes indicates that insulin is successfully forming complex with DPPC liposomes with possibly no pronounced alterations in the structure of insulin molecule.
Keywords:insulin  DPPC  liposomes  FTIR  X-ray diffraction  interaction
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