The Trends in Peptide and Protein Sciences (Trends Pept. Protein Sci.) is a peer-reviewed, online-only (previously print-online), scientific journal owned by Protein Technology Research Center, Shahid Beheshti University of Medical Sciences and documents in all important aspects of the research in peptides and proteins focusing on analytics and impurities, bioinformatics, biopharmaceuticals and vaccines, biotechnology, chemical synthesis, conformational analysis, design and  development of protein therapeutics, determination of structure, enzymology, folding and sequencing,  formulation and stability, function, genetics,  immunology, kinetics, modeling, molecular biology, pharmacokinetics and pharmacodynamics of therapeutic proteins and antibodies, pharmacology,  protein engineering and development, protein-protein interaction, proteomics, purification/expression/production, simulation, thermodynamics and  hydrodynamics and protein biomarkers. The aim of this Journal is to publish high quality original research articles, reviews, short communications and letters and to provide a medium for scientists and researchers to share their findings from the area of peptides and proteins. The Trends in Peptide and Protein Sciences is published in collaboration with Iranian Association of Pharmaceutical Scientists.

The Trends in Peptide and Protein Sciences has been granted the Scientific-Research Rank  by the Commission of Medical Sciences Journals of Ministry of Health, Treatment and Medical Education of I.R. Iran.

 

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Journal Info

Publisher:

Protein Technology Research Center, Shahid Beheshti University of Medical Sciences

Journal Name:

Trends in Peptide and Protein Sciences (TPPS)

Journal Abbreviation:

Trends Pept. Protein Sci.

eISSN:

2538-2446

Chairperson:

Reza Aboofazeli; PhD

Editor-in-Chief:

Bahram Kazemi; PhD

Managing Editor:

Maryam Tabarzad; PhD

Email:

TEL:

File:WhatsApp.svg - Wikipedia WhatsApp:

tipps@sbmu.ac.ir

+98 21 88648124 (8 a. m. to 4 p. m. Tehran, GMT+3.30)

+98 9380414297

linkedin.com/in/journal-trends-in-peptide-and-protein-sciences-314817216

Call for Papers: Electronic Volume 7 (2022)

We are pleased to invite your manuscript submissions to the electronic volume 7 (2022) of Trends in Peptide and Protein Sciences (TPPS). Based on the new TPPS publication policies, articles will be continuously published online only from 2018 ....

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Indexing in Indexcopernicus (ICI Journals Master List)

We would like to inform that the journal „Trends in Peptide and Protein Sciences (ISSN: 2538-2535)” has passed the evaluation process positively and is indexed in the ICI Journals Master List database for 2019 . Based on the information submitted in the evaluation and the analysis of the issues of the journal from 2019, Index Copernicus Experts calculated TPPS Index Copernicus Value (ICV) for 2019. ICV 2019 = 74.91

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Expression of the Mouse HSP27 Chaperone in CHO-K1 Cells for the Enhancement of Viable Cell Density in Batch Culture

Mohammad Reza Amini, Azam Rahimpour, Reyhaneh Hoseinpoor, Masoumeh Rajabibazl

Trends in Peptide and Protein Sciences, Vol. 7 (2022), , Page 1-5 (e2)

Chinese hamster ovary (CHO) cells are extremely vulnerable to cell viability loss in culture despite the availability of different nutrients supplementation strategies. As a result, extending the culture lifetime can profoundly increase recombinant protein expression. Overexpression of HSP27 and its anti-apoptotic effects have been shown in human cell lines in previous studies. In the current study, mouse HSP27 (mHSP27) was cloned in pcDNA 3.1 hygro expression vector and was expressed in CHO-K1 cells to assess its impacts on cell viability and growth. Expression of mHSP27 in CHO-K1 cells was confirmed using RT-PCR. A 3-fold enhancement in peak viable cell density of mHSP27 transfected clones was observed, and culture viability loss was delayed by 2 days compared to un-transfected cells. In future studies, the resulting mHSP27 CHO-K1 cells could be employed as a novel host system for the transient and stable expression of therapeutic recombinant proteins.


HIGHLIGHTS


  • Cell engineering is an effective strategy to cope with apoptosis in CHO cells.

  • HSP27 is involved in mammalian cell apoptosis.

  • Expression of the mouse HSP27 increased the viability and cell density of CHO-K1 cells.

Preparation and In Vitro Characterization of Crocin-loaded Casein Hydrogels

Fatemeh Mehryab, Fatemeh Taghizadeh, Azadeh Haeri

Trends in Peptide and Protein Sciences, Vol. 7 (2022), , Page 1-9 (e3)

Crocin, the main active constituent of saffron, has many important biological activities. Due to its anti-inflammatory properties, crocin can be potentially effective in different pathological conditions including oral ulcers. Novel drug delivery systems such as hydrogels have been used to increase the stability of crocin and provide a controlled release of this compound. Casein is the main protein of milk that possesses suitable properties for the fabrication of hydrogels. In this paper, casein-based hydrogels with different casein to crocin weight ratios were synthesized using the acid-gelation method. The prepared crocin-loaded hydrogels were characterized regarding their rheological behavior, drug content, swelling ratio, surface morphology, thermal stability, and in vitro release profile. The structure of casein hydrogels was characterized using Fourier transform infrared and X-ray diffraction. All formulations exhibited a pseudoplastic rheological behavior and there was no statistically significant difference in viscosity among them. Hydrogel with casein to crocin weight ratio of 10:1 had larger pores and demonstrated a higher swelling percentage and suitable thermal stability. All casein-based hydrogels demonstrated a slow release of crocin over 24 hours and the hydrogel with lower casein to crocin weight ratio had an increased release rate. Taken together, casein-based hydrogels were found to be effective carriers to provide a controlled release system for crocin delivery.


HIGHLIGHTS


  • Casein-based hydrogels were developed for delivery of crocin.

  • Casein-based hydrogels provided a controlled in vitro release profile for crocin.

  • Hydrogel with a lower casein ratio exhibited a higher release rate of crocin.

Controversy Between In Vitro Biological Activities of a Novel Designed Antimicrobial Peptide and Its In Silico Predicted Activities

Fariba Fathi , Maryam Ghobeh , Arash Mahboubi, Maryam Tabarzad

Trends in Peptide and Protein Sciences, Vol. 7 (2022), , Page 1-12 (e4)

Due to their unique mechanisms of action, antimicrobial peptides (AMPs) are promising candidates to combat different infectious diseases. They usually non-specifically interact with the bacterial cell membrane, create pores in their membrane and increase its permeability which causes the death of pathogens. In the design and development of AMPs, in silico strategies have been developed to enhance the function and activity of natural peptides. In this study, in silico approaches were used to develop a novel AMP with several extra bioactivities. Then, the designed AMP were analyzed through computational methods by in vitro experiments. Bioinformatics research revealed a 10-amino-acid peptide (LVSARIRCPK) having antibacterial, anti-biofilm, antiviral, antifungal, and anti-inflammatory effects. However, only the antiviral capabilities of the peptide were validated in the experimental analysis of antibacterial, antifungal, and antiviral activities. This data suggests that; while bioinformatics approaches have greatly advanced in recent years, more optimization work has to be done in order to attain high accuracy and minimize mistakes.


HIGHLIGHTS


  • A novel 10 residues anti-microbial peptide was designed using bioinformatics tools.

  • In vitro analysis showed that this novel AMP did not have efficient antimicrobial activities.

  • Stringencies of bioinformatics criteria thresholds setting may result in better design.

Since the appearance of acquired immunodeficiency syndrome (AIDS) disease, millions of people got infected, thousands are died and many suffered from its complications. One of the chronic and late symptoms of AIDS is lipodystrophy that leads to losing of fat in some parts of the body while gaining it at other organs and sites. One of the main targets in drug development for management of lipodystrophy is growth hormone-releasing hormone (GHRH) receptor. As a secondary metabolite from plants, leginsulin is a peptide with 37 amino acids and considered as hormone-like peptide. In this study, through in silico approaches, binding of leginsulin and GHRH receptor was studied. The results showed strong binding of the two molecules with docking score of -324.16 and ligand RMSD of 47.26. The molecular dynamic investigation also revealed these two proteins remained bound for almost 104 ns. Evaluation of the peptide toxicity in the body had shown that it is not toxic to the human organs and also, it doesn’t pass through the blood brain barrier. The results support the use of legumes as a source of leginsulin for potential management of lipodystrophy in the patients with AIDS.


HIGHLIGHTS


  • Leginsulin is a plant secondary metabolite with 37 amino acids peptide structure.

  • Binding of leginsulin and GHRH receptor was studied through in silico approaches.

  • Results support the leginsulin as a potential management of lipodystrophy in AIDS patients.

Antioxidant Activity of Peptides Derived from Enzymatic Digestion of Spirulina platensis Protein Extract by Different Proteases

Hanieh Niknam, Fariba Fathi, Arash Mahboubi, Maryam Tabarzad

Trends in Peptide and Protein Sciences, Vol. 7 (2022), , Page 1-7 (e6)

One of the attractive sources of bioactive compounds is cyanobacteria and in particular, Chlorella vulgaris and Spirulina platensis. Enzymatic digestion of the Spirulina protein extract can result in bioactive peptides with diverse activities, including antioxidant function. This study aims to produce peptides with antioxidant properties after the enzymatic digestion of Spirulina platensis protein extract using three enzymes: bacterial protease, pepsin, and papain. The protein extract from Spirulina platensis was subjected to enzyme hydrolysis for 3 hours at 37°C (pH 7.4 for papain and bacterial protease and pH 5 for pepsin). The concentration of peptide fragments was evaluated to determine the yield of protein digestion. In order to measure the level of anti-oxidative potential of the hydrolysates, the DPPH assay was run. The results indicated that the bacterial protease led to the highest concentration of peptide fragments, while the hydrolysate obtained from pepsin digestion showed the most antioxidant activity (80%), mainly the peptides that have molecular weights less than 14 KDa. Consequently, pepsin can be a proper enzyme to produce antioxidant peptides from the protein extract of S. platensis. In conclusion, the results of the study confirmed that the products of enzymatic digestion by different enzymes have distinct features.


HIGHLIGHTS


  • Spirulina platensis protein extract was digested with three types of protease.

  • Digestion of protein extract by pepsin resulted in higher antioxidant activity.

  • Digestion by bacterial protease from Bacillus licheniformis resulted in higher yield of peptide formation.

Cytoplasmic Expression of Human Bone Morphogenetic Protein-7 by a Genetically Engineered Strain of Escherichia coli, SHuffle® Strain

Alireza Dugmehchi, Ghazal Sadipour, Yeganeh Talebkhan, Hoda Jahandar, Fahimeh Nemati, Elham Mohit, Leila Nematollahi

Trends in Peptide and Protein Sciences, Vol. 7 (2022), , Page 1-7 (e7)

Homodimeric bone morphogenetic protein-7 (BMP-7) plays a key role in bone metabolism. The functionality of human BMP-7 protein is dependent on its disulfide bond formation and proper folding. Therefore, the expression of soluble recombinant BMP-7 using Escherichia coli cells as the host remains a challenge. Given the need for these disulfide-bonded proteins for stabilized native conformation, the cytoplasm of SHuffle® T7 Express as an E. coli engineered strain can effectively fold disulfide-bonded proteins with a need for proper oxidative folding. These cellular features turn the SHuffle® expression system into an efficient host for the recombinant production of human BMP-7 protein. A soluble dimeric form of recombinant human BMP-7 (rhBMP-7) which has a wide range of applications in medicine and can be used in the treatment of bone defects was produced using the SHuffle® strain as the expression system. This study demonstrated the production of rhBMP-7 using E. coli SHuffle® T7 Express strain. Also, an effective protocol was proposed for the expression and purification of soluble human BMP-7. In addition, it was found that the genetically engineered SHuffle® strain can efficiently enhance the solubility of recombinant human BMP-7 as a therapeutic target.


HIGHLIGHTS                                                             


  • E. coli SHuffle® T7 Express strain is an effective host to express disulfide-bonded proteins.

  • BMP-7 is involved in the process of bone formation.

  • Expression of human BMP-7 in SHuffle® strain increased its solubility.

 

Synthesis, Radiolabeling and Stability Studies of Peptide HYNIC-LIKKP-Pyr-F with 99mTc as an Apoptosis Imaging Agent

Elmira Javani Jouni, Mohammadsaeed Kordi, Sepideh Khoshbakht, Salimeh Amidi , Soraya Shahhosseini

Trends in Peptide and Protein Sciences, Vol. 7 (2022), , Page 1-5 (e8)

A non-invasive method for detecting phosphatidylserine (PS) exposure on the outer surface of plasma membranes, such as nuclear imaging, could aid in the diagnosis and treatment of diseases associated with apoptosis. Annexin V has been the most researched imaging agent for apoptosis to date. Due to Annexin V's limitations, additional agents, such as small peptides and molecules, have been introduced, including LIKKPF developed by Burtea et al. In this study, HYNIC-LIKKP-pyr-F, a derivative of LIKKPF was prepared using the 9-fluoroenylmethoxycarbonyl (fmoc) method, radiolabeled with Technetium-99m (99mTc) with the use of Stannous chloride (SnCl2) as a reducing agent and ethylenediamine diacetate (EDDA) and tricine as co-ligands. Radiochemical purity, labeling efficiency, and stability of radiopeptide in normal saline and human plasma were determined using thin layer chromatography (TLC). The partition coefficient of radiolabeled peptide was measured in a combination of PBS (pH 7.4) and n-octanol. Specific activity was also measured. LC-MS was used to examine the synthesized peptide. Peptide was stable in human serum for at least 4 hr. Peptide was radiolabeled with 99mTc with radiochemical purity and labeling efficiency over 95% and 90%, respectively. Radiopeptide was stable in saline and human serum for at least 4 hours. The radiolabeled peptide has a great deal of potential as an apoptosis imaging agent for in vitro and in vivo experiments.


HIGHLIGHTS


  • A noninvasive method for apoptosis imaging is the usage of radiolabeled affinity ligands.

  • A new derivative of LIKKPF with affinity for phosphatidyl serine was synthesized.

  • The LIKKPF peptide was radiolabeled with 99m

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