scholarly journals Effect of aqueous extracts of aspen, black currant, folded blackberry and walnut leaves on development of pathogenic fungi

2017 ◽  
Vol 38 (SI 2 - 6th Conf EFPP 2002) ◽  
pp. 623-625
Author(s):  
E. Stompor-Chrzan

The antifungal activity of water extracts of dried leaves of folded blackberry (Rubus plicatus W. et N.), walnut (Juglans regia L.), black currant (Ribes nigrum L.), and aspen (Populus tremula L.) was assessed in the in vitro experiment. The tested fungi were Alternaria alternata, Botrytis cinerea, Rhizoctonia solani, Fusarium culmorum, F. oxysporum and F. solani. It was found that all tested extracts inhibited the development of A. alternaria and F. oxysporum, whereas the strongest inhibiting effect was exhibited by extracts of aspen (A. alternata and F. oxysporum), black current (A. alternata) and folded blackberry (F. oxysporum). The tested extracts had no effect on B. cinerea.

2019 ◽  
Vol 16 (4) ◽  
pp. 307-313 ◽  
Author(s):  
Nasrin Zarkar ◽  
Mohammad Ali Nasiri Khalili ◽  
Fathollah Ahmadpour ◽  
Sirus Khodadadi ◽  
Mehdi Zeinoddini

Background: DAB389IL-2 (Denileukin diftitox) as an immunotoxin is a targeted pharmaceutical protein and is the first immunotoxin approved by FDA. It is used for the treatment of various kinds of cancer such as CTCL lymphoma, melanoma, and Leukemia but among all of these, treatment of CTCL has special importance. DAB389IL-2 consists of two distinct parts; the catalytic domain of Diphtheria Toxin (DT) that genetically fused to the whole IL-2. Deamidation is the most important reaction for chemical instability of proteins occurs during manufacture and storage. Deamidation of asparagine residues occurs at a higher rate than glutamine residues. The structure of proteins, temperature and pH are the most important factors that influence the rate of deamidation. Methods: Since there is not any information about deamidation of DAB389IL-2, we studied in silico deamidation by Molecular Dynamic (MD) simulations using GROMACS software. The 3D model of fusion protein DAB389IL-2 was used as a template for deamidation. Then, the stability of deamidated and native form of the drug was calculated. Results: The results of MD simulations were showed that the deamidated form of DAB389IL-2 is more unstable than the normal form. Also, deamidation was carried by incubating DAB389IL-2, 0.3 mg/ml in ammonium hydrogen carbonate for 24 h at 37o C in order to in vitro experiment. Conclusion: The results of in vitro experiment were confirmed outcomes of in silico study. In silico and in vitro experiments were demonstrated that DAB389IL-2 is unstable in deamidated form.


2010 ◽  
Vol 198 (1-3) ◽  
pp. 23-27 ◽  
Author(s):  
Luca Morini ◽  
Alessandra Zucchella ◽  
Aldo Polettini ◽  
Lucia Politi ◽  
Angelo Groppi

2018 ◽  
Vol 56 (4) ◽  
pp. 391 ◽  
Author(s):  
Da-Won Suh ◽  
Young-Kyun Kim ◽  
Yang-Jin Yi

PLoS ONE ◽  
2014 ◽  
Vol 9 (11) ◽  
pp. e113004 ◽  
Author(s):  
Yu Zhang ◽  
Lois Maignien ◽  
Alina Stadnitskaia ◽  
Pascal Boeckx ◽  
Xiang Xiao ◽  
...  

2009 ◽  
Vol 27 (7) ◽  
pp. 961-969 ◽  
Author(s):  
Nicole Mascheri ◽  
Rohan Dharmakumar ◽  
Zhuoli Zhang ◽  
Tatjana Paunesku ◽  
Gayle Woloschak ◽  
...  

2009 ◽  
Vol 16 (2) ◽  
pp. 168-177 ◽  
Author(s):  
Stefan Müller-Hülsbeck ◽  
Philipp J. Schäfer ◽  
Nikolas Charalambous ◽  
Silvio R. Schaffner ◽  
Martin Heller ◽  
...  

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