Specific Strategies for One-Step and Simultaneous Immobilization-Purification of Lipases

Somaye Imanparast, Javad Hamedi, Mohammad Ali Faramarzi

Trends in Peptide and Protein Sciences, Vol. 2 No. 1 (2017), , Page 1-7
https://doi.org/10.22037/tpps.v2i1.19561

Lipases are the biocatalysts with outstanding prospects in industry and medicine. They have proven to be useful in various hydrolytic and synthetic reactions. However, there are some limitations for impure lipases that may restrict their widely uses in industrial applications. Purification is sometimes vital for the characterization of the function, structure, and interactions of lipases. The lipase immobilization is also an efficient strategy for increasing the enzyme activity and stability, and getting a simpler recovery. Lipases are naturally produced together with many other proteins that they may occupy some surface of immobilization solid support and decrease the final activity. The coupling of immobilization and purification of lipase will overcome the mentioned problems and obtain the maximum purification yields. The present mini-review will discuss the use of the techniques that permit to join immobilization and purification of lipases in a single step, including control of the immobilization conditions by interfacial activation on hydrophobic supports, the development of specific supports with affinity for lipases, and the use of bio-affinity supports including immuno- and lectin affinity

HIGHLIGHTS
•Lipases are the biocatalysts with outstanding prospects in industry and medicine.
•Simultaneous immobilization-purification may enhance lipase activity and stability.
•Lipases have a mechanism of interfacial activation in the presence of hydrophobic interfaces.
•The lipase immobilization on hydrophobic supports is a much-utilized strategy.
•Bio-affinity is a promising approach to increase lipase final yield and activity.

Peptide and Protein Interaction Prediction and Intervention with Computational Methods

Newsha Fallah, Saeed Siavashy, Nasim Ghaemian, Farshad Bahramian, Fatemeh Ghorbani-Bidkorbeh

Trends in Peptide and Protein Sciences, Vol. 2 No. 1 (2017), , Page 8-14
https://doi.org/10.22037/tpps.v2i1.19412

Proteins are the most fascinating multifaceted biomacromolecules in living systems and play various important roles such as structural, sensory, catalytic, and regulatory function. Protein and peptide interactions have emerged as an important and challenging topic in
biochemistry and medicinal chemistry. Computational methods as promising tools have been utilized to predict protein and peptide interactions in order to intervene in the biochemical processes and facilitate pharmaceutical peptide design and clarify the complications. This review will introduce the computational methods which are applicable in protein and peptide interaction prediction and summarizes the most successful examples of computational methods described in the literature.

HIGHLIGHTS
•Highlights the importance of peptides and proteins interactions.
•Summarizes the computational methods which are applicable in peptide and protein interaction prediction.
•Highlights the applications of computational methods in peptides and proteins interactions.

Phage Therapy as a New Approach in Treating Emerging Antibiotic Resistant Infections

Ramak Ajideh, Mohammad Ali Faramarzi, Mohammad Hossein Yazdi, Mohammad Reza Pourmand

Trends in Peptide and Protein Sciences, Vol. 2 No. 1 (2017), , Page 15-23
https://doi.org/10.22037/tpps.v2i1.19662

Despite the progress in treatment of infectious diseases, ability of microorganisms to develop the resistance to routine antibiotics has still remained as a big global challenge in clinics. This subject matter keeps the infections top in the list of life threatening diseases especially in those individuals suffering from nosocomial infections. The importance of this global health challenge urges researchers to find an alternative solution with more efficacies to treat infections. There are some alternative approaches by which the global spread of resistant bacteria could be controlled. Through these ways, using bacteriophages instead of different generation of antibiotics brings many promises. According to results of different studies using bacteriophages in the management of infectious disease especially in nosocomial infections not only helps to reduce the spread of antibiotics resistance but also raises the hopes for the rescue of the suffering patients. Bacteriophages can open a new therapeutic window in the control and the treatment of the infectious disease with better efficacy.


HIGHLIGHTS
•Bacteriophage can be used as an antimicrobial agent for treatment of bacterial infection.
•Bacterial resistance to routine antibiotics is a big challenge in the world.
•Specificity toward bacteria is one of the important characteristic of phages.

Ionic Liquids and their Toxicity on the Enzyme Activity and Stability

Mehdi Mogharabi-Manzari, Tabassom Sedaghat-Anbouhi, Mahbobeh Vahidi, Mohammad Ali Faramarzi

Trends in Peptide and Protein Sciences, Vol. 2 No. 1 (2017), , Page 24-34
https://doi.org/10.22037/tpps.v2i1.19580

Molecular interactions are crucial between the enzyme molecules and the surrounding solution in an enzymatic catalysis. Although aqueous solutions used as conventional enzymatic reaction media, non-aqueous enzymology emerges as a major area of biotechnology research and development. Ionic liquids, as new generation of promising alternatives to traditional organic solvents, possess potential industrial enzymatic applications. Enzymes in ionic liquids present enhanced activity, stability, and selectivity. In addition, the potential of ionic liquids in bio-catalysis is raised by high ability of dissolving a wide variety of substrates and their extensively tunable solvent properties through appropriate modification of the cations and anions. However, despite the bio-friendly nature of ionic liquids for enzymatic reactions, their growing interests increase concerns associated with toxicity and environmental pollution of such compounds. This mini-review presents a brief highlight of the contemporary knowledge of enzymes activity and stability in ionic liquids and the environmental influences regarding the potential risks related to the growing applications of these green solvents.

HIGHLIGHTS
•Conventional organic solvents can be replaced by ionic liquids as green solvents.
•Ionic liquids are used as additives, catalysts, or reaction media in industries.
•Advantages and disadvantages of ionic liquids are discussed.
•Potential environmental hazards linked to application of ionic liquids are highlighted.
•The environmental fate needs to be considered in designing safer ionic liquids.

Selection of Efficient Inhibitors for Caspas-9 according to Structure-Based Pharmacophore Screening Strategy and Molecular Dynamics Simulations

Samira Ansari, Ali Naghi Kamali, Kowsar Bagherzadeh, Masoud Amanlou, Sajjad Aghabalazadeh

Trends in Peptide and Protein Sciences, Vol. 2 No. 1 (2017), , Page 35-43
https://doi.org/10.22037/tpps.v2i1.19189

Caspases are enzymes which are the main pathways for apoptosis. Any irregulation in their functions causes increase or decrease in cell death, which result in autoimmune disease or cancer, respectively. In this study, structure-based pharmacophore drug discovery method as a virtual screening was used to discover selective inhibitors for caspase-9. This enzyme is an initiator caspase that is the main pathway in Alzheimer’s disease. A pharmacophore model was developed by investigating essential interactions among the reported potent inhibitors employing a docking analysis methodology. Applying pharmacophore virtual screening, nine compounds from both National Cancer Institute (NCI), and ZINC databases were filtered as potent inhibitors of caspase-9. The efficiency of the discovered compounds was further investigated by docking studies.

HIGHLIGHTS
•Caspase-9 is an important enzyme for apoptosis and its activity is pivotal in cell death.
•A computational design of small molecular inhibitors for caspase-9 performed by structure-based pharmacophore model.
•9 compounds from both National Cancer Institute (NCI) and ZINC databases were discovered as potent inhibitors.

Design and Production of a Novel Polypeptide with Immunogenic Potentials for Immunoassay of Brucella Melitensis

Sahel Hossein Sharghi, Parviz Pakzad Pakzad, Mojgan Bandehpour

Trends in Peptide and Protein Sciences, Vol. 2 No. 1 (2017), , Page 44-48
https://doi.org/10.22037/tpps.v2i1.19360

Brucellosis is one of the most common diseases in humans and it has a worldwide spread. The design and production of newly synthesized proteins can be served as a goal for the rapid and accurate detection of brucellosis. To this aim, finding the antigenic epitopes is the first step to design a diagnostic method. In this study, the epitope mapping procedure was carried out by IEDB analysis resource using Flagellin and Porin amino acid sequences. The selected sequences were linked by GS linkers and cloned into pET26b vector. After confirmation of the expressed recombinant polypeptide by western blotting, it was immunologically analyzed by gel diffusion assay. The SDS PAGE and western blot analysis confirmed the 27 KDa polypeptide production and observing an arc in gel diffusion test demonstrated the precipitation of serum antibodies and the presence of specific antigen complexes. The results showed that the recombinant polypeptide produced in E. coli BL21, could interact with antibodies present in Brucella immunized sheep serum.


HIGHLIGHTS
•Prediction of antigenic epitopes for Brucella membrane proteins.
•Production of designed polypeptide in E. coli BL21 (DE3).
•Interaction of produced polypeptide with Brucella specific antibodies.