Thermoresponsive poly(N-vinylcaprolactam) cryogels: synthesis and its biophysical evaluation for tissue engineering applications.

Summary of "Thermoresponsive poly(N-vinylcaprolactam) cryogels: synthesis and its biophysical evaluation for tissue engineering applications."

The thermoresponsive poly(N-vinylcaprolactam) (PVCl) based cryogel network were synthesized and characterized with respect to physical and biological properties. The PVCl cryogel crosslinked with polyethylene glycol-diacrylate (PEGda) was synthesized in 1% dimethyl sulfoxide containing aqueous medium at -12 degrees C for 12-14 h. The cryogel synthesized in this manner were highly spongy in nature and can absorb water in its porous network. These polymeric cryogel networks have good physical morphology as confirmed by scanning electron microscopy. The estimated porosity of these cryogels was 90% as demonstrated by various methods based on absorption of water and cyclohexane. The median pore diameter and surface area was 30 mum and 2.0253 m(2)/g, respectively as confirmed by analysis on mercury porosimeter. These materials can interact with biological system without any cytotoxic effects. Change in temperature influenced the adsorption of fetal bovine serum (FBS) on PVCl scaffold which showed maximum protein adsorption at 37 degrees C, as compared to that at 25 degrees C. Furthermore, the fibroblast cell adhesion studies showed the potential of these PVCl based cryogels as tissue engineering scaffolds.


Department of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, 208016, Kanpur, India.

Journal Details

This article was published in the following journal.

Name: Journal of materials science. Materials in medicine
ISSN: 1573-4838


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A poly(A) binding protein that is involved in promoting the extension of the poly A tails of MRNA. The protein requires a minimum of ten ADENOSINE nucleotides in order for binding to mRNA. Once bound it works in conjunction with CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR to stimulate the rate of poly A synthesis by POLY A POLYMERASE. Once poly-A tails reach around 250 nucleotides in length poly(A) binding protein II no longer stimulates POLYADENYLATION. Mutations within a GCG repeat region in the gene for poly(A) binding protein II have been shown to cause the disease MUSCULAR DYSTROPHY, OCULOPHARYNGEAL.

Proteins that bind to the 3' polyadenylated region of MRNA. When complexed with RNA the proteins serve an array of functions such as stabilizing the 3' end of RNA, promoting poly(A) synthesis and stimulating mRNA translation.

A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.

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