Result of an experiment shows that when we block NH2 functional groups in RGD peptide, Integrin proteins lose the ability to attach to them, so could I claim that attachment of cell in NH2 modified nanofibrous scaffolds is due to interaction of Integrin proteins of cell membrane with these amine groups?
The results could suggest that. Your hypothesis would be best supported as long as the amine groups on cellular proteins are not being affected (depending on experimental design) and if the scaffold remains intact after treatment. Are you able to test functional groups of the cell proteins after putting them in the scaffold? Do you have a way to test the integrity of the scaffold after treatment?
Hi Mojtaba, if you are just using the RGD tripeptide, then anything bigger that an acetyl group at the N-terminus could be interfering with the integrin binding.
From these results it cannot be assumed that the NH2 groups interact with integrin, since the method of blocking them may be the cause of the reduced/inhibited binding – it is a possible explanation but it cannot be assumed without further investigation.
Not exactly so, It also depends upon the nanofiber dimension and the cell type. For example, endothelial cells shown to have better attachment when they grown over 320 nanometer diameter range of fibers as they get highest possibility of contact guidance. It also depends on the hydrophilic nature of scaffold and porosity to accommodate the cells.
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