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Hindi Research Article
Interplay between Peptide Length, Ionic Strength and pH in Electrophoretic eparations of Polyglutamate
Neeraja Venkateswaran1, Joshua M Kogot2 and Sumita Pennathur1*1Department of Biomolecular Science and Engineering, University of California, Santa Barbara, CA, USA
2Naval Surface Warfare Center, Panama City Division, Science and Technology Department, Panama City FL, USA
- *Corresponding Author:
- Sumita Pennathur
Department of Biomolecular Science and Engineering
University of California, Santa Barbara, CA, USA
Tel: 805-893-5510
E-mail: sumita@engr.ucsb.edu
Received date: October 11, 2015; Accepted date: November 03, 2015; Published date: November 10, 2015
Citation: Venkateswaran N, Kogot JM, Pennathur S (2015) Interplay between Peptide Length, Ionic Strength and pH in Electrophoretic Separations of Polyglutamate. J Anal Bioanal Tech S13:004. doi:10.4172/2155-9872.S13-004
Copyright: © 2015 Venkateswaran N, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
A fundamental study of peptide transport behavior provides information about length dependent transport and sequence structure relationships. In these highly accurate investigations of peptide electrokinetic properties and peptide conformations using a Micro-Electro-Mechanical Systems (MEMS)-fabricated capillary zone electrophoresis (CZE) platform, we demonstrate accurate and repeatable separations of polyglutamate peptides of two different lengths (10 and 20 amino acids). We investigate this separation phenomenon as a function of electrolyte concentration and ionic composition, counter-ion radius, ionic strength and pH. We report a length-dependent counter-ion species selectivity and enhanced separation at pH much higher than the pKa of the peptides that can aid in understanding the relationship between the function of biological peptides and their microenvironments. The ability of our platform to optimize separation resolution between very similar peptides is promising for distinguishing molecular characteristics of peptides and can contribute to resolving current challenges in peptidomics.
