Banca de QUALIFICAÇÃO: STELLA FREITAS DE QUEIROZ

Uma banca de QUALIFICAÇÃO de DOUTORADO foi cadastrada pelo programa.
STUDENT : STELLA FREITAS DE QUEIROZ
DATE: 04/08/2023
TIME: 14:00
LOCAL: por videoconferência
TITLE:

PURIFICATION, PARTIAL CHARACTERIZATION AND EVALUATION OF DALECTIN ANTIMICROBIAL ACTIVITY OF BEARWELL OF Abarema cochliacarpos (GOMES 1803) BARNEBY & GRIMES1996

KEY WORDS:

Medicinal plant, barbatimão, lectin, antimicrobial activity.

PAGES: 82
BIG AREA: Ciências Biológicas
AREA: Bioquímica
SUBÁREA: Química de Macromoléculas
SPECIALTY: Proteínas
SUMMARY:

Several plants are used by man for therapeutic use and propagated over generations. Currently there is a growth in research seeking to identify and isolate active substances present in these organisms in order to create new drugs. The production of the active principles of these organisms is related to their defense mechanism against external agents. These substances are normally classified into primary and secondary metabolites. Lectins are proteins of primary metabolism that can assume several biological roles, including antibacterial, antifungal, anti-inflammatory, antitumor and healing activities. These activities are related to the ability of lectins to bind to carbohydrates present on the cell surface of target organisms, preventing their development and/or inducing a cellular response. Abarema cochliacarpos (Gomes) Barneby & Grimes, popularly known as barbatimão, is a plant used in folk medicine to treat ulcers, wounds, skin rejection, gastritis, among others. This study aims to purify, characterize and evaluate the antimicrobial activity of the inner bark lectin of A. cochliacarpos. that are not of interest. Proteins of interest were eluted with 1M acetic acid. Then a sample was dialyzed to remove the eluting solution and its haemagglutinating activity was evaluated (512). From then on it was called AcBL (A. cochliacarpos bark lectin). It was possible to confirm the purification of the lectin through SDS-PAGE electrophoresis under reducing and non-reducing conditions; the gel showed the presence of a protein band in both conditions. Protein dosage was performed at all stages of purification, as well as characterization tests. AcBL was inhibited by casein, showed thermostability in a wide temperature range, proved to be an acid-neutral protein and had its activity reduced in the presence of EDTA, calcium and magnesium ions. AcBL showed antibacterial activity against A. baumannii, E. faecalis, E. coli, K. pneumoniae, S. enteritidis and S. pyogenes, as well as antifungal activity against C. neoformans, and can be applied as an alternative in the treatment of diseases caused by pathogenic microorganisms. The development of this work contributes to the isolation of new antimicrobial proteins, with regional relevance when investigating lectins from a medicinal plant in Northeast Brazil, which may represent a new biomaterial with high biotechnological potential.

BANKING MEMBERS:
Presidente - 2089586 - FRANCIS SOARES GOMES
Interno(a) - 1612086 - ENIO JOSE BASSI
Interno(a) - 1811274 - HUGO JUAREZ VIEIRA PEREIRA
Externo(a) ao Programa - 1120583 - EDMA CARVALHO DE MIRANDA
Externo(a) à Instituição - POLLYANNA MICHELLE DA SILVA