Showing posts with label misfolding. Show all posts
Showing posts with label misfolding. Show all posts

Tuesday, 31 January 2023

New Protein Settings to Support In vivo Antimalarial Activity in Plasmodium berghei Infected Mice after Garlic-Arteether Therapy: A Recent Study| Chapter 4 | Research Advances in Microbiology and Biotechnology Vol. 2

 WHO is influencing many Control and eradication strategies for ensuing malaria removal in endemic nations. These mechanics challenges necessitate the development of joined approaches, among that safe and effective sickness vaccines could be a critical finish. Due to lack of malaria vaccine, the control works relay chiefly on the   Chemotherapy, especially treatment established traditional medicine has enhance very popular.  Since groupie has developed resistance to all existent antimalarials, the control efforts relay laboriously on treatment accompanying new antimalarial agents preferably pursuing newer targets.  Garlic is individual such established medicine for curing many ailments in Ayurvedic Science. This chapter highlights the antimalarial venture of garlic in combination with artemisinin through a host bootlickers specific protein, peptidyl-prolyl-cis-trans isomerase A (PPIA) in the shielded serum.  It has been illustrated to mediate specific protein closing processes in both artificial and in vivo settings, including the interconversion of the cis and trans. According to the study, overexpressed PPIA can cause parasite proteins that are essential for parasite duplication to misfold, which manage result in parasite humanness or protect samples that have been discussed with a merger of drugs.

Author(s) Details:

Vathsala Palakkod Govindan,
Undergraduate Programme, Indian Institute of Science, Bengaluru, India.

Please see the link here: https://stm.bookpi.org/RAMB-V2/article/view/9221

Friday, 11 June 2021

Study on the Characteristics of α-Chymotrypsin Folding Intermediates by Hydrophobic Interaction Chromatography (HIC) | Chapter 2 | Current Advances in Chemistry and Biochemistry Vol. 7

The study of protein folding intermediates is crucial for understanding the folding mechanism of denatured proteins and enhancing protein folding efficiency. A new methodology to define the intermediate of urea-denatured -chymotrypsin (-Chy) was established in this study by using some of the linear parameters of the stoichiometric displacement theory of retention of solute (SDT-R) of hydrophobic interaction chromatography (HIC). As urea concentration (Curea) fluctuates, the contact surface region (Z, S), affinity (logI), and character of interaction force (j) of the -Chy to the stationary phase of HIC (STHIC) between the intermediate (M) and native (N) states were shown to be considerably different. With modifications in Curea, a linear relationship between logI and Z was discovered only for its N state, not for its M state, implying that the interaction force between -Chy in N state and the STHIC is non-selective in N state but selective in M state. In addition, the magnitude of both logI and Z measured in the M state is only a fifth of that in the N state. To discriminate between proteins in the N and M states, all three parameters were used. This finding could be used to distinguish any non-functional protein with a correct three- or four-dimensional molecular structure from their stable M state of any kind of protein, and/or other proteins, in proteome research, protein separation, and a thorough understanding of the intrinsic rule of protein folding in molecular biology.

Author (s) Details

Congyu Ke
College of Chemistry and Chemical Engineering, Xi’an Shiyou University, Xi,’an 710065, China.

Wei Tuo
Schol of Foreign Languages, Xi’an Shiyou University, Xi’an 710065, China.

Wujuan Sun
College of Chemistry and Chemical Engineering, Xi’an Shiyou University, Xi,’an 710065, China.

Jianjun Li
Institute of Modern Separation Science, Shaanxi Key Laboratory of Modern Separation Science, Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Northwest University, 710069 Xi’an, P.R. China.

Zhenling Liu
Xinxiang Medical College, Xinxiang, 453003, Henan Province, P.R. China.

Xindu Geng
Institute of Modern Separation Science, Shaanxi Key Laboratory of Modern Separation Science, Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Northwest University, 710069 Xi’an, P.R. China.

View Book :- https://stm.bookpi.org/CACB-V7/article/view/1188