Abstract
Understanding peptide-membrane interaction in view of structural change of lipid bilayer is essential to develop new therapeutic strategies. Though different mechanisms are proposed for cell penetrating peptides (CPPs) penetration in lipid bilayer, the exact mechanism of cellular uptake of CPPs remains a significant unanswered piece of puzzle. Here, we report a novel observation that model phospholipid vesicles self-reproduce to generate unilamellar daughter vesicles in presence of a CPP, nonaarginine (R9). Fluorescence lifetime image analysis (FLIM) exquisitely captures the changes of L-α-phosphatidylcholine (LAPC) bilayer in different times and also quantifies the changes through valuable lifetime distributions obtained. Mean square displacement (MSD) calculations from FLIM images of single vesicle trajectory establish CPP induced self-reproduction of LAPC vesicles. Heterogeneous nature of lipid bilayer after 1 hour of R9 addition is observed from fluorescence correlation spectroscopy (FCS) which supposed to consider as the starting point of “mother vesicles” reproduction. Solvation dynamic study delineates the change in dynamics of the encapsulated water inside vesicles which also states different rigidity of lipid bilayer in different states of vesicle self-reproduction. Fluorescence anisotropy image analysis provides information regarding change in lipid bilayer rigidity by quantifying the rotational motion of the fluorophore in presence of perturbation of CPPs. From these experimental observations, we are able to establish phospholipid vesicles self-reproduction in presence of CPPs which may be considered as a possible route of CPPs action to deliver cargos to cell interior through hydrophobic barriers. Overall, our results provide an experimental underpinning of the role of lipid bilayer structural changes in self-reproduction which can exhibit great potential to interpret the protein-lipid interaction in emergence of life.
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