scholarly journals 5-amino levulinic acid inhibits SARS-CoV-2 infection in vitro

2021 ◽  
Vol 545 ◽  
pp. 203-207
Author(s):  
Yasuteru Sakurai ◽  
Mya Myat Ngwe Tun ◽  
Yohei Kurosaki ◽  
Takaya Sakura ◽  
Daniel Ken Inaoka ◽  
...  
Keyword(s):  
Levulinic Acid ◽  
Amino Levulinic Acid

The influence of storage conditions on delta amino levulinic acid induced toxicity and phototoxicity in vitro

2006 ◽  
Vol 3 (1) ◽  
pp. 35-45 ◽  
Author(s):  
Aurelie Furiga ◽  
David Olivier ◽  
Marc Baud’huin ◽  
Ludovic Bourre ◽  
Andresz Bugaj ◽  
...  
Keyword(s):  
Levulinic Acid ◽  
Storage Conditions ◽  
Amino Levulinic Acid

scholarly journals 5-amino levulinic acid inhibits SARS-CoV-2 infection in vitro

2020 ◽  
Author(s):  
Yasuteru Sakurai ◽  
Mya Myat Ngwe Tun ◽  
Yohei Kurosaki ◽  
Takaya Sakura ◽  
Daniel Ken Inaoka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dietary Supplement ◽  
Causative Agent ◽  
Levulinic Acid ◽  
Antiviral Drug ◽  
Anticancer Therapy ◽  
Antiviral Effects ◽  
Amino Levulinic Acid ◽  
High Bioavailability

AbstractThe current COVID-19 pandemic requires urgent development of effective therapeutics. 5-amino levulinic acid (5-ALA) is a naturally synthesized amino acid and has been used for multiple purposes including as an anticancer therapy and as a dietary supplement due to its high bioavailability. In this study, we demonstrated that 5-ALA treatment potently inhibited infection of SARS-CoV-2, a causative agent of COVID-19. The antiviral effects could be detected in both human and non-human cells, without significant cytotoxicity. Therefore, 5-ALA is a candidate as an oral antiviral drug for COVID-19.

scholarly journals Studies on the Biosynthesis of Heme from Iron and Protoporphyrin

Blood ◽  
1959 ◽  
Vol 14 (4) ◽  
pp. 486-497 ◽  
Author(s):  
H. C. SCHWARTZ ◽  
G. E. CARTWRIGHT ◽  
EMIL L. SMITH ◽  
M. M. WINTROBE
Keyword(s):  
Particulate Matter ◽  
Levulinic Acid ◽  
Reduced Glutathione ◽  
Enzyme Concentration ◽  
Chicken Erythrocyte ◽  
Heme Synthesis ◽  
Enzyme Solution ◽  
Optimal Stability ◽  
Amino Levulinic Acid

Abstract 1. Additional evidence has been presented that the formation of heme in vitro from iron and protoporphyrin is enzyme dependent. 2. An enzyme solution was prepared from the active particulate matter of a chicken erythrocyte hemolysate. The enzyme is soluble in 0.15 M KCl and optimally active at pH 7.9. 3. The rate of heme synthesis was constant over the first 30 minutes and approached maximal values at 3 to 4 hours. At optimal concentrations of protoporphyrin and iron the rate of heme synthesis over the first 30 minutes was proportional to enzyme concentration. 4. The enzyme solution was 89 per cent inactivated after heating at 56 C. for 30 minutes. Optimal stability for 3 hours was at pH 7.4. It was unstable when lyophilized or on storage at 5 C. or -30 C. 5. The enzyme was inhibited by 1 x 10-2 M p-chloromercuriphenylsulfonate and 1 x 10-2 M iodoacetamide. 6. There was a 70 per cent loss of activity after dialysis of the enzyme solution for 22 hours against water. The dialyzed enzyme solution was reactivated with either reduced glutathione or cysteine. 7. The enzyme solution augmented heme synthesis in vitro from δ-amino-levulinic acid, porphobilinogen and protoporphyrin, but not from glycine.

Photodynamic Therapy of Normal and Balloon-Injured Rat Carotid Arteries Using 5-Amino-Levulinic Acid

Circulation ◽  
1995 ◽  
Vol 91 (2) ◽  
pp. 417-425 ◽  
Author(s):  
Isaac Nyamekye ◽  
Sandra Anglin ◽  
Jean McEwan ◽  
Alexander MacRobert ◽  
Stephen Bown ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Levulinic Acid ◽  
Carotid Arteries ◽  
Amino Levulinic Acid

scholarly journals FINE STRUCTURAL CHANGES IN PROPLASTIDS DURING PHOTODESTRUCTION OF PIGMENTS

1964 ◽  
Vol 22 (2) ◽  
pp. 443-451 ◽  
Author(s):  
Shimon Klein ◽  
Lawrence Bogorad
Keyword(s):  
Fine Structure ◽  
Levulinic Acid ◽  
Structural Changes ◽  
Prolamellar Body ◽  
Membrane Structures ◽  
Lamellar Structures ◽  
Amino Levulinic Acid ◽  
Stroma Lamellae ◽  
Green Pigments ◽  
Bean Leaves

Etiolated bean leaves supplied δ-amino-levulinic acid in the dark synthesize large amounts of protochlorophyllide which is not converted to chlorophyllide upon illumination of the leaves. The fine structure of the proplastids is not affected by the treatment. When leaves containing "inactive" protochlorophyllide are exposed to light of 700 ft-c for 3 hours, they lose practically all their green pigments. During this period large stacks of closed membrane structures are built up in the region of the prolamellar body. These lamellar structures remain even when no or only traces of pigment are left in the leaves. In untreated control leaves the pigment content remained constant during similar illumination and the structural changes in the plastids consisted of a rearrangement of the vesicles from the prolamellar bodies into strands dispersed through the stroma; lamellae and grana formation occurred later.

Protoheme formation in barley in response to light, dark and delta‐amino levulinic acid

1984 ◽  
Vol 7 (1-5) ◽  
pp. 807-818
Author(s):  
Ibraheem M. Ameen ◽  
Gene W. Miller
Keyword(s):  
Levulinic Acid ◽  
Amino Levulinic Acid
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