Author

Sam Sung

ORCID Identifier(s)

0009-0009-0842-0898

Graduation Semester and Year

2023

Language

English

Document Type

Dissertation

Degree Name

Doctor of Philosophy in Chemistry

Department

Chemistry and Biochemistry

First Advisor

Daniel W Armstrong

Abstract

Amino acids are essential building blocks in all life on Earth. It was first mistakenly believed that only L-amino acids were of biological relevance in higher organisms, and D-amino acids were laboratory artifacts or biologically irrelevant. It is well accepted today that various D-amino acids exist in different organisms, including humans, and some even play critical roles in biological pathways and processes. In addition, aberrant levels of certain D-amino acids have been reported in patients with varying diseases. It has been proposed that the aberrant variations in the levels of D-amino acids in biological fluids may serve as biomarkers for disease in humans. However, due to the lack of a comprehensive and robust analytical platform a full understanding of D-amino acids remains elusive and most of D-amino acids and their biological roles are not well investigated. An analytical challenge is the analysis of D-amino acids in biological samples, because dominant L-amino acid signals and a mix of other endogenous compounds can interference with detection and quantitation of the trace analytes of interest. Additionally, current methods for the comprehensive analysis of D-amino acids are time consuming. Therefore, the main goals of this dissertation are to a) enhance the sensitivity of current analytical methods and platforms for D-amino acid analysis in biological samples, and b) provide information and methodologies that future studies can use to investigate the roles of D-amino acids in biological systems. A comparison between using UV, MS single quad, multiple reaction monitoring (MRM) detection modes was investigated to determine limits of detection (LOD) for the analysis of AQC-amino acids. This achiral method showed improved detection sensitivity as low as pg and sub-pg levels when using high sensitivity detection modes such as MRM and fluorimetry. A separate study reported the first comprehensive analysis of the intracellular and extracellular profiles of L- and D-amino acid in human breast cancer cells (MCF-7) and non-tumorigenic epithelial breast cells (MCF10A) using HPLC-MS/MS. This study further advanced our knowledge of how D-amino acids can interact with the NMDA receptors in cancer cells. For the differentiation of peptides containing D-amino acids, a novel enzymatic technique using carboxypeptidase Y, coupled with selective retention of D-amino acids and D-amino acid containing peptides on teicoplanin type stationary phases was developed. This enzyme hydrolytically cleaves L-amino acids at the peptide bond from the C-terminus of peptides, but its catalytic efficiency decreases dramatically when confronted with a C-terminal D-amino acid. The strong retention of D-amino acids and D-amino acid containing peptides on teicoplanin stationary phases was then exploited to analyze intact fragments of the carboxypeptidase hydrolysis by LC-MS/MS with little to no interference from more abundant L-amino acid peptides. A fully comprehensive, highly sensitive and selective 2D-HPLC-MS/MS chiral separation method was developed along with a complementary GC-MS/MS method for the study of L- and D-homoserine lactone homologues in the extracellular media of gram-negative bacteria.

Keywords

D-amino acids, D-amino acid containing peptides, AQC-derivatization, carboxypeptidase Y, teicoplanin aglycone, homoserine lactones, HPLC, LC-MS/MS, chiral separations.

Disciplines

Chemistry | Physical Sciences and Mathematics

Comments

Degree granted by The University of Texas at Arlington

31252-2.zip (2909 kB)

Included in

Chemistry Commons

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.