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Biomolecule-Nanomaterial Interactions: Effect on Biomolecular Structure, Function, and Stability

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Biological Interactions on Materials Surfaces

Abstract

We have characterized the influence of protein–carbon nanotube interactions on protein structure and function using various techniques such as Fourier transform infrared spectroscopy, circular dichroism spectroscopy, and atomic force microscopy. This structure-based analysis revealed that different proteins interact with nanotubes differentially, consistent with the observed biological activity data. Furthermore, the high degree of surface curvature of the nanoscale support was found to play an important role in stabilizing proteins under denaturing conditions. Along with these fundamental studies, various applications of such highly active and stable nanotube–protein conjugates have been pursued, which include self-cleaning nanobiocomposite films, interfacial biocatalysis in a biphasic medium, and synthesis of nanotube–nanoparticle hybrids, among others.

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Abbreviations

ADH:

alcohol dehydrogenase

AFM:

atomic force microscopy

AGP:

α1-acid glycoprotein

AOT:

Aerosol-OT

BSA:

bovine serum albumin

CALB:

Candida antarctica lipase B

CD:

circular dichroism

CNT:

carbon nanotube

CT:

α-chymotrypsin

d-SBP:

deglycosylated soybean peroxidase

EDC:

N-ethyl-N′-(3-dimethylaminopropyl) carbodiimide hydrochloride

EDX:

energy dispersive X-ray

FAM:

carboxyfluorescein

FT-IR:

Fourier transform infrared

HOPG:

highly ordered pyrolytic graphite

HRP:

horseradish peroxidase

HSA:

human serum albumin

Lys:

lysozyme

MJL:

Mucor javanicus lipase

MWNT:

multiwalled nanotube

NaDDBS:

sodium dodecylbenzene sulfonate

NHS:

N-hydroxysuccinimide

NIR:

near infrared

PAGE:

polyacrylamide gel electrophoresis

PLL:

poly-l-lysine

PMMA:

poly(methyl methacrylate)

PMSF:

phenylmethansulfonyl fluoride

ROS:

reactive oxygen species

SAM:

self-assembled monolayer

SBP:

soybean peroxidase

SC:

subtilisin Carlsberg

SWNT:

single-walled nanotube

TEM:

transmission electron microscopy

TRY:

trypsin

UV:

ultraviolet

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Authors and Affiliations

  1. Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA

    Ravindra C. Pangule, Shyam Sundhar Bale, Dhiral A. Shah, Amit Joshi, Prashanth Asuri, Jonathan S. Dordick & Ravi S. Kane

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  1. Ravindra C. Pangule
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  2. Shyam Sundhar Bale
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    Pangule, R.C. et al. (2009). Biomolecule-Nanomaterial Interactions: Effect on Biomolecular Structure, Function, and Stability. In: Puleo, D., Bizios, R. (eds) Biological Interactions on Materials Surfaces. Springer, New York, NY. https://doi.org/10.1007/978-0-387-98161-1_5

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