Influence of functionalized nanoparticles on conformational stability of type I collagen for possible biomedical applications.

Collagen-nanoparticle interactions are vital for many biomedical applications including drug delivery and tissue engineering applications. Iron oxide nanoparticles synthesized using starch template according to our earlier reported procedures were functionalized by treating them with Gum Arabic (GA), a biocompatible polysaccharide, so as to enhance the interaction between nanoparticle surfaces and collagen. Viscosity, circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) techniques have been used to study the collagen-nanoparticle interactions. The relative viscosity for collagen-nanoparticle conjugate was found to increase with increase in concentration of the nanoparticle within the concentration range investigated, which is due to the aggregation of protein onto the surface of nanoparticle. The CD spectra for the collagen-nanoparticle at different concentration ratios do not have much variation in the Rpn values (ratio of positive peak intensity over negative peak intensity) after functionalization with GA. The variation of molar ellipticity values for collagen-nanoparticle is due to the glycoprotein present in GA. The collagen triple helical structure is maintained after interaction with nanoparticles. The FTIR spectra of native collagen, Coll-Fs (nanoparticle without functionalization) and Coll-FsG (nanoparticle functionalized with GA) show clearly the amide I, II, III bands, with respect to collagen. The ability of polysaccharide stabilized/functionalized nanoparticles to maintain the collagen properties would help in its biomedical applications.

Dielectric behaviour and conformational stability of collagen on interaction with DNA.

Collagen-DNA interaction studies will aid in improving the stability of DNA against nucleases. In the present study, the effect of DNA on different physico-chemical properties of collagen like viscosity, conformation and dielectric behaviour has been studied. Increase of DNA concentration leads to the increment of viscosity of collagen at the pH 4 and 5, but the trend is reversed at the pH of 6 and 7 due to the formation of collagen fibrils. The temperature dependent CD spectroscopic studies for collagen-DNA conjugate showed that thermal stability of collagen is modulated with increasing molar concentration of DNA. It also shows that DNA interactions with collagen did not result in change in the triple helical structure of collagen. Impedance measurements show that the strength of ion pairs for different molar concentrations of collagen-DNA conjugates has changed. Nyquist plot for collagen-DNA conjugate posses higher Y″ at DNA concentration of 1:25 and 1:50 whereas at 1:1 and 1:10 lower Y″ than the native collagen have been observed. An understanding of this nature of the collagen-DNA interactions is helpful for gene delivery applications.