Bruno M. GuerreiroUniversidade NOVA de Lisboa | NOVA · Center for Biotechnology and Fine Chemicals (CQFB/REQUIMTE)
Bruno M. Guerreiro
PhD Student @ FCT-NOVA
Cryobiology, isochoric biopreservation, polymer chemistry, computational thermodynamics, stochastic nucleation theory
About
12
Publications
984
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31
Citations
Introduction
Researcher with a strong biochemistry background.
Interested in bio-based polysaccharide applications, cryopreservation and molecular dynamics.
Skills and Expertise
Additional affiliations
February 2019 - March 2019
Position
- Research Undergraduate Program Mentor
Description
- Mentored Ana Filipa Veríssimo on her PIPP (10607) course, part of the MEng Biomedical Engineering curriculum, which led to her project "Sugar-protein content determination by spectroscopic techniques"
January 2019 - present
September 2018 - January 2019
Position
- Professor (Assistant)
Description
- Participated in the Biomolecular Spectroscopy (10805) course, part of the MSc Biochemistry curriculum. Held Raman & Fluorescence lab classes and mentored 4 students on their final project "Fluorescence study on BSA interaction with ibuprofen and caffeine"
Education
September 2016 - September 2018
September 2013 - September 2016
Publications
Publications (12)
Reactive oxygen species (ROS) are dangerous sources of macromolecular damage. While most derive from mitochondrial oxidative phosphorylation, their production can be triggered by exogenous stresses, surpassing the extinction capacity of intrinsic antioxidant defense systems of cells. Here, we report the antioxidant activity of FucoPol, a fucose-ric...
This study reports the performance of FucoPol, a fucose-containing bacterial polysaccharide, as a photostable agent with high absorption yield at concentrations as low as 0.02% (w/v). FucoPol is non-cytotoxic, efficiently protects from UVA and UVB at concentrations of 0.02–2% (w/v) and 0.2–2% (w/v), respectively, has over 94% overall photostability...
We report the cryoprotective potential of FucoPol, a fucose-containing bacterial exopolysaccharide produced by Enterobacter A47. In vitro cryopreservation assays of Vero, Saos-2, HFFF2 and C2C12 cell lines exposed to a validated non-cytotoxic 2.5 mg/ml FucoPol concentration demonstrated a consistent post-thaw metabolic viability increase. Calorimet...
Cryopreservation of biological tissue has had a big spotlight in the field of medicine, as it aims for long-term storage of whole organs for transplantation and constant improvement of biobanking methodologies. However, current procedures still struggle with cryoprotectant cytotoxicity, optimal freeze-thaw rates and efficient carrier formulas. The...
(B.Sc. thesis upload for documentation purposes only) Cryopreservation allows organisms to survive at sub-zero temperatures by making use of biological agents able to control crystal growth and avoid lethal damage. Artificial cryopreservation has been widely optimized and used in the food industry and for medical applications, most recently to prov...
Questions
Questions (3)
I performed a deproteinization of my biopolysaccharide and performed a Bradford assay on the native and deproteinized versions of the polymer to quantify purification yield.
What happened is that the deproteinized polymer contains MORE protein than the native polymer, as inferred by its higher absorbance at 595nm post-Bradford.
Is there any sort of interference that may cause this? Because I checked UV-VIS earlier and the 280 nm protein band disappeared in the deproteinized polymer.
I'm experimenting biopolymer reducing power and currently I am following the method of Oyaizu et al. 1986.
However, when doing my positive control of ascorbic acid, I get higher reducing power for lower concentrations.
The curve is similar to a titration, it has an inflexion point around 0.6% w/v ascorbic acid, but decreases with increasing concentrations.
Anyone ever got this result? I can't backtrack the problem.
I am trying to evaluate BSA denaturation state with GdnHCl by fluorescence emission. I'm using 0,25mg/ml BSA with a neutral density filter of OD= 1,0 and excitation wavelength 285 nm. My method is to titrate from 0 to 3M GdnHCl to obtain a sinusoidal denaturation curve, but when I tried 3M GdnHCl to see if I would get a saturated signal, fortunately I didn't. But the native protein (on an intensity scale of 1-1000) showed intensity of 480 and 3M denatured solution had an intensity of 485 (only +5, which is about 1%). Can anyone see what might be the problem AND: theoretically BSA uncoils when denatured, so tryptophans should fluoresce more. However, some articles say they suffer quenching from solution molecules. So what is the answer?
Projects
Project (1)
To develop biopolymers tailored for a cryoprotective setting and evaluate the molecular dynamics involved.
