Protection of Oxygen-Sensitive Enzymes by Peptide Hydrogel

ACS Nano ◽  
2021 ◽  
Author(s):  
Oren Ben-Zvi ◽  
Itzhak Grinberg ◽  
Asuka A. Orr ◽  
Dror Noy ◽  
Phanourios Tamamis ◽  
...  
Keyword(s):  
Oxygen Sensitive ◽  
Peptide Hydrogel

scholarly journals Nanostructure, Self-Assembly, Mechanical Properties, and Antioxidant Activity of a Lupin-Derived Peptide Hydrogel

Biomedicines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 294
Author(s):  
Raffaele Pugliese ◽  
Anna Arnoldi ◽  
Carmen Lammi
Keyword(s):  
Mechanical Properties ◽  
Antioxidant Activity ◽  
Self Assembly ◽  
Antioxidant Activities ◽  
Functional Materials ◽  
Cd Spectroscopy ◽  
Beneficial Effects ◽  
Naturally Occurring ◽  
New Research ◽  
Peptide Hydrogel

Naturally occurring food peptides are frequently used in the life sciences due to their beneficial effects through their impact on specific biochemical pathways. Furthermore, they are often leveraged for applications in areas as diverse as bioengineering, medicine, agriculture, and even fashion. However, progress toward understanding their self-assembling properties as functional materials are often hindered by their long aromatic and charged residue-enriched sequences encrypted in the parent protein sequence. In this study, we elucidate the nanostructure and the hierarchical self-assembly propensity of a lupin-derived peptide which belongs to the α-conglutin (11S globulin, legumin-like protein), with a straightforward N-terminal biotinylated oligoglycine tag-based methodology for controlling the nanostructures, biomechanics, and biological features. Extensive characterization was performed via Circular Dichroism (CD) spectroscopy, Fourier Transform Infrared spectroscopy (FT-IR), rheological measurements, and Atomic Force Microscopy (AFM) analyses. By using the biotin tag, we obtained a thixotropic lupin-derived peptide hydrogel (named BT13) with tunable mechanical properties (from 2 to 11 kPa), without impairing its spontaneous formation of β-sheet secondary structures. Lastly, we demonstrated that this hydrogel has antioxidant activity. Altogether, our findings address multiple challenges associated with the development of naturally occurring food peptide-based hydrogels, offering a new tool to both fine tune the mechanical properties and tailor the antioxidant activities, providing new research directions across food chemistry, biochemistry, and bioengineering.

scholarly journals Engraftment of strictly anaerobic oxygen-sensitive bacteria in irritable bowel syndrome patients following fecal microbiota transplantation does not improve symptoms

Gut Microbes ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 1-16
Author(s):  
Patrick Denis Browne ◽  
Frederik Cold ◽  
Andreas Munk Petersen ◽  
Sofie Ingdam Halkjær ◽  
Alice Højer Christensen ◽  
...  
Keyword(s):  
Irritable Bowel Syndrome ◽  
Fecal Microbiota Transplantation ◽  
Fecal Microbiota ◽  
Strictly Anaerobic ◽  
Oxygen Sensitive ◽  
Irritable Bowel

scholarly journals Clostridium haemolyticum Infection: A Cause of Hemolytic Anemia in a Patient with Bone Marrow Necrosis

2021 ◽  
Vol 9 (8) ◽  
pp. 1568
Author(s):  
Anne Sophie Lagneaux ◽  
Sandrine Hénard ◽  
Laure Diancourt ◽  
Emmanuelle Stein ◽  
Pierre Perez ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Hemolytic Anemia ◽  
Obese Woman ◽  
Molecular Techniques ◽  
Significant Past Medical History ◽  
Bone Marrow Necrosis ◽  
Rdna Sequencing ◽  
Oxygen Sensitive ◽  
Bacteremic Episode ◽  
Bone Marrow Regeneration

Clostridium haemolyticum is a sporulating Gram-positive anaerobic rod that is considered to be one of the most fastidious and oxygen-sensitive anaerobes. It is a well-known animal pathogen and the cause of bacillary hemoglobinuria primarily in cattle. To date, human infections caused by C. haemolyticum have been reported in three patients with malignant underlying diseases. We present herein the case of a 30-year-old obese woman with no significant past medical history who developed bacteremia caused by C. haemolyticum with massive intravascular hemolysis associated with bone marrow necrosis and acute renal failure. Because of subculture failure, the diagnosis was made on the basis of 16S rDNA sequencing and next-generation sequencing. The patient, who had been afebrile for 20 days after a 17-day-course of antibiotics, experienced a second bacteremic episode caused by C. haemolyticum. After having been successfully treated for 42 days with clindamycin and amoxicillin-clavulanic acid, the patient developed acute myeloid leukemia as a result of bone marrow regeneration. Although uncommon in humans, infections caused by C. haemolyticum are severe and should be considered in a febrile patient who has severe hemolytic anemia. This case also highlights the importance of using molecular techniques for the identification of this fastidious anaerobic organism.

scholarly journals Improving gelation efficiency and cytocompatibility of visible light polymerized thiol-norbornene hydrogels via addition of soluble tyrosine

2017 ◽  
Vol 5 (3) ◽  
pp. 589-599 ◽  
Author(s):  
Han Shih ◽  
Hung-Yi Liu ◽  
Chien-Chi Lin
Keyword(s):  
Visible Light ◽  
Peptide Hydrogel

A biomimetic PEG-peptide hydrogel was developed through tyrosine-assisted visible-light thiol-norbornene crosslinking. Soluble tyrosine improves crosslinking and enhances the cytocompatibility of hydrogels.

Real-Time Monitoring of Dissolved Oxygen with Inherent Oxygen-Sensitive Centers in Metal–Organic Frameworks

2016 ◽  
Vol 28 (8) ◽  
pp. 2652-2658 ◽  
Author(s):  
Jian Yang ◽  
Zhe Wang ◽  
Yongsheng Li ◽  
Qixin Zhuang ◽  
Jinlou Gu
Keyword(s):  
Dissolved Oxygen ◽  
Real Time ◽  
Metal Organic Frameworks ◽  
Real Time Monitoring ◽  
Oxygen Sensitive ◽  
Metal Organic

scholarly journals Protein Import into Hydrogenosomes of Trichomonas vaginalis Involves both N-Terminal and Internal Targeting Signals: a Case Study of Thioredoxin Reductases

2008 ◽  
Vol 7 (10) ◽  
pp. 1750-1757 ◽  
Author(s):  
Marek Mentel ◽  
Verena Zimorski ◽  
Patrick Haferkamp ◽  
William Martin ◽  
Katrin Henze
Keyword(s):  
Trichomonas Vaginalis ◽  
Protein Import ◽  
Atp Synthesis ◽  
Antioxidant Systems ◽  
Low Oxygen ◽  
Oxygen Sensitive ◽  
Targeting Signal ◽  
Targeting Signals ◽  
Thioredoxin Reductases

ABSTRACT The parabasalian flagellate Trichomonas vaginalis harbors mitochondrion-related and H2-producing organelles of anaerobic ATP synthesis, called hydrogenosomes, which harbor oxygen-sensitive enzymes essential to its pyruvate metabolism. In the human urogenital tract, however, T. vaginalis is regularly exposed to low oxygen concentrations and therefore must possess antioxidant systems protecting the organellar environment against the detrimental effects of molecular oxygen and reactive oxygen species. We have identified two closely related hydrogenosomal thioredoxin reductases (TrxRs), the hitherto-missing component of a thioredoxin-linked hydrogenosomal antioxidant system. One of the two hydrogenosomal TrxR isoforms, TrxRh1, carried an N-terminal extension resembling known hydrogenosomal targeting signals. Expression of hemagglutinin-tagged TrxRh1 in transfected T. vaginalis cells revealed that its N-terminal extension was necessary to import the protein into the organelles. The second hydrogenosomal TrxR isoform, TrxRh2, had no N-terminal targeting signal but was nonetheless efficiently targeted to hydrogenosomes. N-terminal presequences from hydrogenosomal proteins with known processing sites, i.e., the alpha subunit of succinyl coenzyme A synthetase (SCSα) and pyruvate:ferredoxin oxidoreductase A, were investigated for their ability to direct mature TrxRh1 to hydrogenosomes. Neither presequence directed TrxRh1 to hydrogenosomes, indicating that neither extension is, by itself, sufficient for hydrogenosomal targeting. Moreover, SCSα lacking its N-terminal extension was efficiently imported into hydrogenosomes, indicating that this extension is not required for import of this major hydrogenosomal protein. The finding that some hydrogenosomal enzymes require N-terminal signals for import but that in others the N-terminal extension is not necessary for targeting indicates the presence of additional targeting signals within the mature subunits of several hydrogenosome-localized proteins.

scholarly journals Slow-Release RGD-Peptide Hydrogel Monoliths

Langmuir ◽  
2012 ◽  
Vol 28 (34) ◽  
pp. 12575-12580 ◽  
Author(s):  
Valeria Castelletto ◽  
Ian W. Hamley ◽  
Christopher Stain ◽  
Che Connon
Keyword(s):  
Slow Release ◽  
Rgd Peptide ◽  
Peptide Hydrogel
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