Development of new mass spectrometry techniques and their general applications in science: chemistry, biochemistry, material sciences, forensics, medicine, food science, pharmaceutical and veterinary medicine

• Grant number: 13/23920-8
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• Start date: September 01, 2014
• End date: October 31, 2015
• Field of knowledge: Physical Sciences and Mathematics - Chemistry - Organic Chemistry
• Principal Investigator: Marcos Nogueira Eberlin
• Grantee: Lygia de Azevedo Marques
• Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• Associated research grant: 10/51677-2 - Development of new mass spectrometry techniques and their general applications in science: chemistry, biochemistry, material sciences, forensics, medicine, food science, pharmaceutical and veterinary medicine, AP.TEM

Abstract

Since its infancy, mass spectrometry (MS) has been directly involved in major scientific developments. From the discovery of the electron and the isotopes, and nuclear energy, to the recent and extraordinary developments in protein characterization, the MS technique has provided Science with a very diverse and useful set of tools. During the last two decades, with the development of revolutionary ionization techniques and new instruments, the MS technique has experienced even more intense and extraordinary growth, being today an indispensable technique in various fields in Science. The ThoMSon Mass Spectrometry Laboratory at the Institute of Chemistry - University of Campinas - UNICAMP, has been since 1992 very active in the development of new MS techniques and new MS applications, and is placed today among the most active and productive MS research groups worldwide. The ThoMSon lab has been very active, with great emphasis via multidisciplinary collaborations with national and Internacional groups, in the formation of a new generation of Brazilian experts in MS. This thematic project has therefore the objective to consolidate and expand the leading role of the ThoMSon lab in the development of new MS techniques and applications. The project also opens new research areas such as those related to studies on hormones, forensic science and bacterial screening. A variety of research proposals are described in diverse areas: applications of ambient mass spectrometry (EASI-MS) in chemistry and forensic chemistry; characterization of coordination and supramolecular organo-mettalic species via ESI-MS/MS; ion/molecule reaction studies via pentaquadrupole mass spectrometry; monitoring of the destruction of pollutants in solution via ESI-MS/MS and V-EASI-MS; differentiation of constitutional isomers and enantiomers via TWIM-MS; fringerprinting of complex chemical mixtures via ESI-MS/MS; new applications of via LC-MS/MS techniques in reproduction and veterinary medicine; and microorganism identification via MALDI-MS. It is expected, therefore, that this thematic project will result in even more intense and higher quality scientific production, and in the more intense formation of highly qualified researchers and professionals in an area which is presently of great relevance and demand in Science and Technology. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

PENA, IZABELLA AGOSTINHO; MARQUES, LYGIA AZEVEDO; LARANJEIRA, ANGELO B. A.; YUNES, JOSE A.; EBERLIN, MARCOS N.; MACKENZIE, ALEX; ARRUDA, PAULO. Mouse lysine catabolism to aminoadipate occurs primarily through the saccharopine pathway; implications for pyridoxine dependent epilepsy (PDE). BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, v. 1863, n. 1, p. 121-128, JAN 2017. (13/23920-8, 10/50114-4, 12/00235-5)

PENA, IZABELLA A.; MARQUES, LYGIA A.; LARANJEIRA, ANGELO B. A.; YUNES, JOSE A.; EBERLIN, MARCOS N.; ARRUDA, PAULO. Simultaneous detection of lysine metabolites by a single LC-MS/MS method: monitoring lysine degradation in mouse plasma. SPRINGERPLUS, v. 5, FEB 25 2016. (13/23920-8, 10/50114-4, 12/00235-5)