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A light scattering study of interactions of oppositely charged proteins in solution

Published online by Cambridge University Press:  01 February 2011

Perumal Radha Ramasamy ,
Raafat Elmaghrabi ,
Gary Halada  and
Miriam Rafailovich
Perumal Radha Ramasamy
Affiliation:
popeye_iit@yahoo.com, SUNY - Stony Brook University, Materials Science and Engineering, 317, Old Engineering Building,, SUNY - Stony Brook University, Stony Brook, NY, 11794 2275, United States, 631 793 0683
Raafat Elmaghrabi
Affiliation:
Raafat.El-Maghrabi@stonybrook.edu, Stony Brook University, Dept of Physiology & Biophysics, T6-170 Health Sciences Center, Stony Brook, NY 11794-8661, Stony Brook, NY, 11794-8661, United States
Gary Halada
Affiliation:
Gary.Halada@stonybrook.edu, Stony Brook University, Materials Science and Engineering, 308 Engineering Building, Stony Brook, NY 11794-2275, Stony Brook, NY, 11794-2275, United States
Miriam Rafailovich
Affiliation:
Miriam.Rafailovich@stonybrook.edu, Stony Brook University, Materials Science and Engineering, 322 Engineering Building, Stony Brook, NY 11794-2275, Stony Brook, NY, 11794-2275, United States
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Abstract

In experiments involving electrophoresis of proteins in gels, it was observed that the mobility of FITC tagged albumin (FITC albumin) was greater than that of TRITC tagged albumin (TRITC albumin). To further understand the effects of tagging proteins with fluorescent dyes, interactions of anionic proteins FITC albumin and untagged bovine serum albumin (BSA), with cationic protein ploy-L-lysine was studied using dynamical light scattering. It was found that aggregates formed by the interaction of FITC albumin with poly-L-lysine were larger than those formed by the interaction between poly-L-lysine and BSA. Using zeta potential measurements it was observed that irrespective of the fluorescent tags attached to them, the zeta potential values of cationic proteins changed from negative to positive with increasing amounts of poly-L-lysine. It was also observed that addition of small amounts of poly-L-lysine to solutions containing FITC albumin decreased the zeta potential drastically. To explain this data, we are proposing a model that suggests that low concentrations of poly-L-lysine serve as scaffold - like structures on which several FITC albumin molecules anchor. We conclude that FITC appears to change the surface charge of albumin significantly and thereby influencing its behavior in solution and its interaction with cationic poly-L-lysine.

Keywords

biologicalelectrical propertiesbiomaterial
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1061: Symposium MM – Biomolecular and Biologically Inspired Interfaces and Assemblies , 2007 , 1061-MM09-24
Copyright
Copyright © Materials Research Society 2008

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