Interaction of L-amino Acids with the Fusion Structures of a Cysteine Proteinase/Cystatin Pair
- Authors: Gholizadeh A.1
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Affiliations:
- Research Institute for Fundamental Sciences (RIFS)
- Issue: Vol 52, No 2 (2016)
- Pages: 143-148
- Section: Article
- URL: https://journal-vniispk.ru/0003-6838/article/view/151864
- DOI: https://doi.org/10.1134/S000368381602006X
- ID: 151864
Cite item
Abstract
In a basic investigation, the molecular interactions between 2 different fused products of Arabidopsis cysteine proteinase (CP) and cysteine proteinase inhibitor (CPI) pair “namely R1: H2N-maltose-binding protein- CPI-CP-COOH and R2: H2N-maltose binding protein-CP-CPI-COOH” and 4 different L-amino acids including L-Ala, L-Ser, L-Asp, and L-Phe were analyzed using experimental methods and computational tools. The activity of CP relatively increased in purified R2 product in which test L-amino acids tend to interact with CP/CPI pair. On the other hand, the functionality of R1 product (having no tendency to interact with CP/CPI pair) was not influenced by L-amino acids. Detection of the effect of L-enantiomers of amino acids on the fusion forms of 2 functionally related proteins such as CP and CPI is the first ever time work on this research area. As a research recommendation, manufacturing the switchable biological systems expressing the fused forms of CP/CPI pair was proposed to control the relative activities of proteolytic compounds in different environments in the future.
Keywords
About the authors
A. Gholizadeh
Research Institute for Fundamental Sciences (RIFS)
Author for correspondence.
Email: aghz_bioch@yahoo.co.in
Iran, Islamic Republic of, Tabriz
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