Effect of ionic liquids on the different hierarchical order of type I collagen

•The effect of imidazolium ILs on the hierarchical order of collagen is atypical.•Secondary structure and fibril formation of collagen is unaffected at molecular level.•Thermal stability of collagen fiber is decreased in the presence of ionic liquids.•Imidazolium ILs reveal increased pore size of th...

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Bibliographic Details
Published in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2014-05, Vol.117, p.376-382
Main Authors: Mehta, Ami, Rao, J. Raghava, Fathima, Nishter Nishad
Format: Article
Language:English
Subjects:
Animals
Circular dichroism (CD)
Collagen
Collagen Type I - chemistry
Collagen Type I - drug effects
Goats
Imidazoles - pharmacology
Imidazolium chloride
Ionic Liquids - pharmacology
Lyotropic action
Porosity
Protein Stability - drug effects
Protein Structure, Secondary
Rats
Room temperature ionic liquids
Scanning electron microscopy (SEM)
Skin - drug effects
Skin - ultrastructure
Spectroscopy, Fourier Transform Infrared
Tail
Temperature
Tendons - chemistry
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Summary:•The effect of imidazolium ILs on the hierarchical order of collagen is atypical.•Secondary structure and fibril formation of collagen is unaffected at molecular level.•Thermal stability of collagen fiber is decreased in the presence of ionic liquids.•Imidazolium ILs reveal increased pore size of the skin, suggesting lyotropic action.•ILs are potential for collagen-based biomaterials that require controlled, desired porosity materials. The effect of ionic liquids (ILs) on proteins has been gaining huge interest due to easy tunability of cation and anion for generating the desired effect. This study explores the effect of alkyl imidazolium chloride ILs on collagen at molecular, inter-fibrillar and skin matrix level. Circular dichroic studies reveal that at the molecular level, the secondary structure of collagen was not affected by imidazolium ILs and there was no change in thermal stability as well. However, collagen at the inter-fibrillar level behaved differently. With increase in concentration of ILs, remarkable decrease in thermal stability of rat tail tendon (RTT) collagen fibers with marginal swelling effect was seen. SEM micrographs of skin matrix treated with IL show opening up of pores. This kind of exquisite behavior of ILs at different hierarchal order of collagen indicates that ILs are endowed with potential lyotropic action, which can be judiciously employed for biomedical applications.
ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2014.03.014