Biomedical subjects

Sandeep S Karajanagi

Publications and source records attributed to Sandeep S Karajanagi.

7 recordsLinked to original sources

PubMed2006

Water-soluble carbon nanotube-enzyme conjugates as functional biocatalytic formulations.

We report the activity, stability, and reusability of enzyme-carbon nanotube conjugates in aqueous solutions. A variety of enzymes were covalently attached to oxidized multi-walled carbon nanotubes (MWNTs). These conjugates were soluble in aqueous buffer, retained a high fraction of their native activity, and were stable at higher temperatures relative to their solution phase counterparts. Furthermore, the high surface area of MWNTs afforded high enzyme loadings, yet the intrinsic high length of the MWNT led to facile filtration. These water-soluble carbon nanotube-enzyme conjugates represent novel preparations that possess the virtues of both soluble and immobilized enzymes, thus providing a unique combination of useful attributes such as low mass transfer resistance, high activity and stability, and reusability.

Biotransformation↗

PubMed2006

The protein-nanomaterial interface.

Developments in the past few years have illustrated the potentially revolutionizing impact of nanomaterials, especially in biomedical imaging, drug delivery, biosensing and the design of functional nanocomposites. Methods to effectively interface proteins with nanomaterials for realizing these applications continue to evolve. Proteins are being used to control both the synthesis and assembly of nanomaterials. There has also been an increasing interest in understanding the influence of nanomaterials on the structure and function of proteins. Understanding and controlling the protein-nanomaterial interface will be crucial for designing functional protein-nanomaterial conjugates and assemblies.

Binding Sites↗

PubMed2006

Increasing protein stability through control of the nanoscale environment.

We have discovered a novel property of single-walled carbon nanotubes (SWNTs)-their ability to stabilize proteins at elevated temperatures and in organic solvents to a greater extent than conventional flat supports. Experimental results and theoretical analysis reveal that the stabilization results from the curvature of SWNTs, which suppresses unfavorable protein-protein lateral interactions. Our results also indicate that the phenomenon is not unique to SWNTs but could be extended to other nanomaterials. The protein-nanotube conjugates represent a new generation of active and stable catalytic materials with potential use in biosensors, diagnostics, and bioactive films and other hybrid materials that integrate biotic and abiotic components.

Adsorption↗

PubMed2006

Protein-assisted solubilization of single-walled carbon nanotubes.

We report a simple method that uses proteins to solubilize single-walled carbon nanotubes (SWNTs) in water. Characterization by a variety of complementary techniques including UV-Vis spectroscopy, Raman spectroscopy, and atomic force microscopy confirmed the dispersion at the individual nanotube level. A variety of proteins differing in size and structure were used to generate individual nanotube solutions by this noncovalent functionalization procedure. Protein-mediated solubilization of nanotubes in water may be important for biomedical applications. This method of solubilization may also find use in approaches for controlling the assembly of nanostructures, and the wide variety of functional groups present on the adsorbed proteins may be used as orthogonal reactive handles for the functionalization of carbon nanotubes.

Journal Article↗

PubMed2006

Directed assembly of carbon nanotubes at liquid-liquid interfaces: nanoscale conveyors for interfacial biocatalysis.

We report that single-walled carbon nanotubes (SWNTs) can be directed to aqueous-organic interfaces with the aid of surfactants. This phenomenon can also be used to transport enzymes to the interface to effect biphasic biotransformations. Consequently, SWNT-enzyme conjugates enhance the rate of catalysis by up to 3 orders of magnitude relative to the rates obtained with native enzymes in similar biphasic systems. Furthermore, we demonstrate that this concept can be extended to other nanomaterials and other enzymes, thereby providing a general strategy for efficient interfacial biocatalysis. The ability to direct the assembly of nanotubes at the interface also provides an attractive route to organizing these nanomaterials into 2D architectures.

Alcohol Dehydrogenase↗

PubMed2004

Structure and function of enzymes adsorbed onto single-walled carbon nanotubes.

We have examined the structure and function of two enzymes, alpha-chymotrypsin (CT) and soybean peroxidase (SBP), adsorbed onto single-walled carbon nanotubes (SWNTs). SBP retained up to 30% of its native activity upon adsorption, while the adsorbed CT retained only 1% of its native activity. Analysis of the secondary structure of the proteins via FT-IR spectroscopy revealed that both enzymes undergo structural changes upon adsorption, with substantial secondary structural perturbation observed for CT. Consistent with these results, AFM images of the adsorbed enzymes indicated that SBP retains its native three-dimensional shape while CT appears to unfold on the SWNT surface. This study represents the first in depth investigation of protein structure and function on carbon nanotubes, which is critical in designing optimal carbon nanotube-protein conjugates.

Animals↗

PubMed2003

Si nanocolumns as novel nanostructured supports for enzyme immobilization.

Silicon nanocolumns have been used as novel supports for the high-density immobilization of enzymes. Silicon nanocolumns with diameters of ca. 50-100 nm and a height of 1 micron were constructed using glancing angle deposition. The surfaces were successively treated with 3-aminopropyltriethoxysilane (APTES) and then with an amine reactive polymer, poly(ethylene-alt-maleic anhydride), to attach soybean peroxidase (SBP) to the support. Optimal coverage of APTES, polymer, and SBP was obtained for incorporation of enzyme onto the sidewalls of the nanocolumns. SBP immobilized on the silicon nanocolumns demonstrated an enhancement in biocatalytic activity of 160% over that of the enzyme immobilized on flat silicon wafers with the same projected area. The enzymatic activity decreased with progressive washes for both supports. This decrease in the activity of enzyme was found to be primarily due to the intrinsic deactivation of immobilized enzyme on the silicon surface. Designing nanocolumns with optimal dimensions, spacing, and surface chemistry may lead to the development of high-density arrays of proteins for applications in biotechnology.

Adsorption↗