Estrutura primária e análise do potencial biotecnológico de uma lectina da alga marinha vermelha Amansia multifida J.V. lamouroux

Abstract

Fifty percent of the biodiversity of the world are in the oceans. The seaweeds are a diverse group of organisms that are the source of bioactive compounds with diverse application for human benefit. Among these compounds are lectins, ubiquitous proteins or glycoproteins with at least one non-catalytic domain binding reversibly to a specific mono- or oligosaccharides. Studies with algae lectin, although still recent when compared to lectins from other organisms, show that these proteins have a wide possibility of biotechnological applications. AIDS, cancer as well infections caused by antibiotic-resistant bacteria are public health problems that kill hundreds of thousands of people each year, lectins from algae have been shown proteins with highly potent activity because of their specificity to carbohydrates high mannose. Because of that, algae lectins have attracted particular attention with regard to studies of antiviral activities, against cancer cells and antibiotic. Furthermore, studies researching antioxidant activity of lectins are underexplored with only one reported with this property. The aim of this study was to determine the primary structure of the Amansia multifida lectin (AML) by combining mass spectrometry, Edman degradation and molecular biology, evaluate its antioxidant activity, biotechnological potential of AML against cancer cells, HIV-I and HIV- II and against growth of bacterial biofilms. The sequence when compared to databases (NCBI) showed homology to lectins belonging to the family OAAH. The results have shown that AML is a protein of OAAH family with four repeated domains in its aminoacid sequence as well as a conserved carbohydrate binding site with high identity with the lectins of OAAH family. AML is the first lectin from red marine alga with antioxidant activity, capable to reduce cell viability of colon cancer cells, it also reduces the number of viable cells of S. aureus and E. coli, and exhibit activity at micromolar concentrations against HIV-I and HIV-II virus.