Jagannath Swaminathan

ORCID: 0000-0002-5005-7182
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About
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Research Areas
  • Advanced Proteomics Techniques and Applications
  • Advanced Biosensing Techniques and Applications
  • Advanced biosensing and bioanalysis techniques
  • Click Chemistry and Applications
  • Crystallization and Solubility Studies
  • Chemical Synthesis and Analysis
  • X-ray Diffraction in Crystallography
  • Genetics, Bioinformatics, and Biomedical Research
  • Nanocluster Synthesis and Applications
  • Single-cell and spatial transcriptomics
  • Mass Spectrometry Techniques and Applications
  • Monoclonal and Polyclonal Antibodies Research
  • Lanthanide and Transition Metal Complexes
  • Magnetism in coordination complexes
  • Adenosine and Purinergic Signaling
  • Biotin and Related Studies
  • Glycosylation and Glycoproteins Research
  • Molecular Sensors and Ion Detection
  • RNA modifications and cancer
  • Polyamine Metabolism and Applications
  • RNA and protein synthesis mechanisms
  • Cancer-related gene regulation
  • Epigenetics and DNA Methylation
  • Supramolecular Self-Assembly in Materials
  • Analytical Chemistry and Chromatography

The University of Texas at Austin
2014-2024

Institut de Biologie Moléculaire et Cellulaire
2016

Koo & Associates International (United States)
2014

Institut de Biologie systémique et synthétique
2014

Vellore Institute of Technology University
2007

The proteomes of cells, tissues, and organisms reflect active cellular processes change continuously in response to intracellular extracellular cues. Deep, quantitative profiling the proteome, especially if combined with mRNA metabolite measurements, should provide an unprecedented view cell state, better revealing functions interactions components. Molecular diagnostics biomarker discovery benefit particularly from accurate quantification proteomes, since complex diseases like cancer...

10.1371/journal.pcbi.1004080 article EN public-domain PLoS Computational Biology 2015-02-25

Lysine dimethylation (Kme2) is a crucial post-translational modification (PTM) that regulates biological processes and implicated in diseases. There significant interest globally identifying these methylation marks. Unfortunately, this remains challenging due to the lack of robust technologies for selectively labeling Kme2. To address this, we present chemical method named tertiary amine coupling by oxidation (TACO). This modifies Kme2 aldehydes using Selectfluor base. The resulting from...

10.1021/jacs.4c00253 article EN cc-by Journal of the American Chemical Society 2024-04-08

Single-molecule protein sequencing is regarded as a promising new method in the field of proteomics. It potentially offers orders magnitude improvements sensitivitiy and throughput for detection when compared to mass spectrometry. However, development such technology faces significant barriers, especially need chemically derivatize specific amino-acid types with unique labels. For example, fluorescent dyes would be suitable single-molecule microscopy or nanopore-based sequencing. These...

10.1039/c6nj02932a article EN New Journal of Chemistry 2016-11-18

Methods for the selective labeling of biogenic functional groups on peptides are being developed and used in workflow both current emerging proteomics technologies, such as single-molecule fluorosequencing. To achieve successful with any one method requires that peptide fragments contain group which chemistry is designed. In practice, only two present every fragment regardless protein cleavage site, namely, an N-terminal amine a C-terminal carboxylic acid. Developing global-labeling...

10.1021/acschembio.1c00631 article EN ACS Chemical Biology 2021-11-04

We report a fast and highly efficient diazonium reaction that couples nitroazobenzene chromophore to tyrosine histidine residues, thus endowing peptides with high photoabsorption cross sections at 351 nm in the gas phase. Only tagged undergo ultraviolet photodissociation (UVPD) nm, as demonstrated for several Tyr- His-containing from protein digests. Additional selectivity is achieved by integration of UVPD-MS method an silico database search restricted peptides. A modified MassMatrix...

10.1021/ac403654m article EN Analytical Chemistry 2014-06-04

The field of proteomics has expanded recently with more sensitive techniques for the bulk measurement peptides as well single-molecule techniques. One limiting factor some these methods is need multiple chemical derivatizations and highly pure proteins free contaminants. We demonstrate a solid-phase capture-release strategy suitable proteolysis, purification, subsequent modification peptides. use this resin on an HEK293T cell lysate perform one-pot capture, derivatization to survey peptide...

10.1021/acschembio.0c00040 article EN ACS Chemical Biology 2020-05-02

Abstract The software Peptide Fragment Ion Analyser (PFIA) aids in the analysis and interpretation of tandem mass spectrometric data peptides. package has been designed to facilitate product ions derived from acyclic cyclic peptide natural products that possess unusual amino acid residues are heavily post‐translationally modified. consists two programmes: (a) PFIA‐I lists compositions their corresponding ion types for ‘a queried m/z value’ ( z = +1) (b) PFIA‐II displays fragmentation pattern...

10.1002/rcm.3179 article EN Rapid Communications in Mass Spectrometry 2007-08-20

Chromophores that incorporate f-block elements have considerable potential for use in bioimaging applications because of their advantageous photophysical properties compared to organic dye, which are currently widely used. We developing new classes lanthanide-based self-assembling molecular nanoparticles as reporters imaging and multi-functional nanoprobes or nanosensors with biological samples. One class these materials, we call lanthanide "nano-drums", homogeneous 4d-4f clusters...

10.1039/c4dt02646b article EN Dalton Transactions 2014-12-02

It has been hypothesized that components of enzymatic pathways might organize into intracellular assemblies to improve their catalytic efficiency or lead coordinate regulation. Accordingly, de novo purine biosynthesis enzymes may form a purinosome in the absence purines, and punctate body identified as purinosome. We investigated mechanism by which human biosynthetic be organized purinosomes, especially under differing cellular conditions. Irregardless activity bodies formed endogenous...

10.1371/journal.pone.0056203 article EN cc-by PLoS ONE 2013-02-06

ABSTRACT The need to accurately survey proteins and their modifications with ever higher sensitivities, particularly in clinical settings limited samples, is spurring development of new single molecule proteomics technologies. Fluorosequencing one such highly parallelized peptide sequencing platform, based on determining the sequence positions select amino acid types within peptides enable identification quantification from a reference database. Here, we describe substantial improvements...

10.1101/2023.09.15.558007 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-09-16

We are developing a new class of lanthanide-based self-assembling molecular nanoparticles as potential reporter molecules for imaging, and multi-functional nanoprobes or nanosensors in diagnostic systems. These lanthanide “nano-drums” homogeneous 4d–4f clusters approximately 25 to 30 Å diameter that can emit from the visible near-infrared (NIR) wavelengths. Here, we present syntheses, crystal structures, photophysical properties, comparative cytotoxicity data six nano-drums containing either...

10.1039/c4fd00117f article EN Faraday Discussions 2014-01-01

ABSTRACT The proteomes of cells, tissues, and organisms reflect active cellular processes change continuously in response to intracellular extracellular cues. Deep, quantitative profiling the proteome, especially if combined with mRNA metabolite measurements, should provide an unprecedented view cell state, better revealing functions interactions components. Molecular diagnostics biomarker benefit particularly from accurate quantification proteomes, since complex diseases like cancer protein...

10.1101/010587 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2014-10-22

A peptide sequencing scheme utilizing fluorescence microscopy and Edman degradation to determine the amino acid position in fluorophore-labeled peptides was recently reported, referred as fluorosequencing. It observed that multiple fluorophores covalently linked a scaffold resulted decrease anticipated output worsened single-molecule analysis. In this study, we report an improvement photophysical properties of by incorporating long flexible (PEG)

10.1021/acs.bioconjchem.2c00103 article EN Bioconjugate Chemistry 2022-05-27

Silica passivating agents have shown great success in minimizing nonspecific protein binding to glass surfaces for imaging and microscopy applications. Amine-derivatized are commonly used conjugation with amide coupling immobilize peptides/proteins through C-terminal or side-chain carboxylic acids. In the case of single-molecule fluorosequencing peptides, attachment occurs via C-terminus surface has previously been a source error peptide identification. Here, we employ as high-throughput,...

10.1021/acs.langmuir.1c02644 article EN Langmuir 2021-12-14

Abstract Methods for the selective labeling of biogenic functional groups on peptides are being developed and used in workflow both current emerging proteomics technologies, such as single-molecule fluorosequencing. To achieve successful with any one method requires that peptide fragments contain group which chemistry is designed. In practice, only two present every fragment regardless protein cleavage site, namely, an N -terminal amine a C carboxylic acid. Developing global-labeling...

10.1101/2021.07.08.451692 preprint EN cc-by-nc bioRxiv (Cold Spring Harbor Laboratory) 2021-07-09

10.5281/zenodo.4989148 article EN Zenodo (CERN European Organization for Nuclear Research) 2021-06-18

10.5281/zenodo.7958185 article EN Zenodo (CERN European Organization for Nuclear Research) 2023-05-22
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