Primary structure of subunit B of the 11S globulin of seeds of cotton plant variety 108-F. I. Acid-soluble peptides from complete tryptic hydrolysis of subunit B

1984 ◽  
Vol 20 (1) ◽  
pp. 83-87
Author(s):  
A. L. Li ◽  
T. S. Yunusov ◽  
�. R. Kal'metova
Keyword(s):  
Cotton Plant ◽  
Primary Structure ◽  
Plant Variety ◽  
11S Globulin ◽  
Subunit B ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis

scholarly journals Performance of the Natural Mortality Factors of Aphis gossypii (Hemiptera: Aphididae) as a Function of Cotton Plant Variety and Phenology

2018 ◽  
Vol 47 (2) ◽  
pp. 440-447 ◽  
Author(s):  
António Chamuene ◽  
Tamíris Alves Araújo ◽  
Gerson Silva ◽  
Thiago Leandro Costa ◽  
Paulo Geraldo Berger ◽  
...  
Keyword(s):  
Cotton Plant ◽  
Aphis Gossypii ◽  
Natural Mortality ◽  
Mortality Factors ◽  
Plant Variety

scholarly journals Targeting PirAvp and PirBvp Toxins of Vibrio parahaemolyticus with Oilseed Peptides: An In Silico Approach

Antibiotics ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 1211
Author(s):  
Joe-Hui Ong ◽  
Wey-Lim Wong ◽  
Fai-Chu Wong ◽  
Tsun-Thai Chai
Keyword(s):  
Complex Formation ◽  
In Silico ◽  
Vibrio Parahaemolyticus ◽  
Water Solubility ◽  
Toxin Binding ◽  
Binding Peptides ◽  
Acute Hepatopancreatic Necrosis Disease ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis ◽  
Dual Target

Acute hepatopancreatic necrosis disease (AHPND), caused by PirAvp- and PirBvp-releasing Vibrio parahaemolyticus strains, has resulted in massive mortality in shrimp aquaculture. Excessive use of antibiotics for AHPND management has led to antibiotic resistance, highlighting the urgency to search for alternatives. Using an in silico approach, we aimed to discover PirAvp/PirBvp-binding peptides from oilseed meals as alternatives to antibiotics. To search for peptides that remain intact in the shrimp digestive tract, and therefore would be available for toxin binding, we focused on peptides released from tryptic hydrolysis of 37 major proteins from seeds of hemp, pumpkin, rape, sesame, and sunflower. This yielded 809 peptides. Further screening led to 24 peptides predicted as being non-toxic to shrimp, fish, and humans, with thermal stability and low water solubility. Molecular docking on the 24 peptides revealed six dual-target peptides capable of binding to key regions responsible for complex formation on both PirAvp and PirBvp. The peptides (ISYVVQGMGISGR, LTFVVHGHALMGK, QSLGVPPQLGNACNLDNLDVLQPTETIK, ISTINSQTLPILSQLR, PQFLVGASSILR, and VQVVNHMGQK) are 1139–2977 Da in mass and 10–28 residues in length. Such peptides are potential candidates for the future development of peptide-based anti-AHPND agents which potentially mitigate V. parahaemolyticus pathogenesis by intercepting PirAvp/PirBvp complex formation.

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