دانلود گزارش کارورزی و کار آموزی

چکیده : 

The role and importance of the conformation of antimicrobial peptides for their binding and incorporation

into lipid membranes as well as for their bioactivity are still not well understood. In this paper, we studied the

interaction between four cationic alpha-helical KLA peptides, which differ primarily in their helical propensity,

and the anionic gel-state lipid DPPG (1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol). Of particular interest

was the influence of the peptide conformation and membrane surface properties on the electrostatic binding

process. Dynamic light scattering (DSL) showed that generally the KLA peptides possess high aggregation

power but modest solubilization power. Circular dichroism spectroscopy (CD) spectra revealed that the KLA

peptides with the low helical propensity tend to form beta-structures at low lipid/peptide ratios. Differential

scanning calorimetry (DSC) thermograms showed that the helical KLA peptides stabilize the DPPG bilayer,

whereas the beta-structured peptides induce pronounced membrane perturbations. Isothermal titration

calorimetry (ITC) isotherms showed that the helical KLA peptides bind more efficiently to DPPG vesicles than