Angiostatic Proteins and Peptides

Currently, drug delivery technologies for protein and peptide delivery mainly rely on biodegradable polymers. However, protein stability during release from these systems can be critical due to physical and chemical instabilities. Lipospheres are solid microparticles composed of fat core stabilized by phospholipids layer represent an alternative carrier for the delivery of highly challenging, labile and unstable substances. This review highlights various aspects of lipospheres like physicochemical characteristics and stability for better clinical utility with a wider spectrum of proteins and peptides.

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Properties and Biotechnological Application of mutant Derivatives of Mini-intein PRP8 from Penicillium chrysogenum with Improved Control of C-terminal Processing

Biotekhnologiya ◽

10.21519/0234-2758-2019-35-6-91-101 ◽

2019 ◽

Vol 35 (6) ◽

pp. 91-101

Author(s):

F.A. Klebanov ◽

S.E. Cheperegin ◽

D.G. Kozlov

Keyword(s):

Penicillium Chrysogenum ◽

Protein Denaturation ◽

Biologically Active ◽

Cultivation Temperature ◽

Target Proteins ◽

E Coli ◽

Complete Inactivation ◽

Target Molecules ◽

Proteins And Peptides

Mutant variants of mini-intein PRP8 from Penicillium chrysogenum (Int4b) with improved control of C-terminal processing were characterized. The presented variants can serve as a basis for self-removed polypeptide tags capable of carrying an affine label and allowing to optimize the process of obtaining target proteins and peptides in E. coli cells. They allow to synthesize target molecules in the composition of soluble and insoluble hybrid proteins (fusions), provide their afnne purification, autocatalytic processing and obtaining mature target products. The presented variants have a number of features in comparison with the known prototypes. In particular the mutant mini-intein Int4bPRO, containing the L93P mutation, has temperature-dependent properties. At cultivation temperature below 30 °C it allows the production of target molecules as part of soluble fusions, but after increasing of cultivation temperature to 37 °C it directs the most of synthesized fusions into insoluble intracellular aggregates. The transition of Int4bPRO into insoluble form is accompanied by complete inactivation of C-terminal processing. Further application of standard protein denaturation-renaturation procedures enable efficiently reactivate Int4bPRO and to carry out processing of its fusions in vitro. Two other variants, Int4b56 and Int4b36, containing a point mutation T62N or combination of mutations D144N and L146T respectively, have a reduced rate of C-terminal processing. Their use in E. coli cells allows to optimize the biosynthesis of biologically active target proteins and peptides in the composition of soluble fusions, suitable for afnne purification and subsequent intein-dependent processing without the use of protein denaturation-renaturation procedures. intein, fusion, processing, processing rate, gelonin The work was supported within the framework of the State Assignment no. 595-00003-19 PR.

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Uterine Wound Healing: A Complex Process Mediated by Proteins and Peptides

Current Protein and Peptide Science ◽

10.2174/1389203717666160322145939 ◽

2016 ◽

Vol 18 (2) ◽

pp. 125-128 ◽

Cited By ~ 11

Author(s):

Dario Lofrumento ◽

Maria Nardo ◽

Marianna Falco ◽

Andrea Lieto

Keyword(s):

Wound Healing ◽

Complex Process ◽

Proteins And Peptides

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Clinical Use of Toxic Proteins and Peptides from Tian Hua Fen and Scorpion Venom

Current Protein and Peptide Science ◽

10.2174/1389203719666180622100641 ◽

2019 ◽

Vol 20 (3) ◽

pp. 285-295

Author(s):

Chen Ling ◽

Yuanhui Zhang ◽

Jun Li ◽

Wenli Chen ◽

Changquan Ling

Keyword(s):

Herbal Medicines ◽

Scorpion Venom ◽

The Other ◽

Western World ◽

Chinese Government ◽

Clinical Use ◽

Potential Benefits ◽

Scientific Results ◽

Proteins And Peptides ◽

Toxic Proteins

Traditional Chinese Medicine (TCM) has been practiced in China for thousands of years. As a complementary and alternative treatment, herbal medicines that are frequently used in the TCM are the most accepted in the Western world. However, animal materials, which are equally important in the TCM practice, are not well-known in other countries. On the other hand, the Chinese doctors had documented the toxic profiles of hundreds of animals and plants thousand years ago. Furthermore, they saw the potential benefits of these materials and used their toxic properties to treat a wide variety of diseases, such as heavy pain and cancer. Since the 50s of the last century, efforts of the Chinese government and societies to modernize TCM have achieved tremendous scientific results in both laboratory and clinic. A number of toxic proteins have been isolated and their functions identified. Although most of the literature was written in Chinese, this review provide a summary, in English, regarding our knowledge of the clinical use of the toxic proteins isolated from a plant, Tian Hua Fen, and an animal, scorpion, both of which are famous toxic prescriptions in TCM.

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Chinese Medicine Protein and Peptide in Gene and Cell Therapy

Current Protein and Peptide Science ◽

10.2174/1389203719666180612082432 ◽

2019 ◽

Vol 20 (3) ◽

pp. 251-264 ◽

Cited By ~ 1

Author(s):

Yinlu Feng ◽

Zifei Yin ◽

Daniel Zhang ◽

Arun Srivastava ◽

Chen Ling

Keyword(s):

Chinese Medicine ◽

Cell Therapy ◽

Future Research ◽

The Past ◽

Promising Strategy ◽

Wide Range ◽

New Directions ◽

Gene And Cell Therapy ◽

Proteins And Peptides

The success of gene and cell therapy in clinic during the past two decades as well as our expanding ability to manipulate these biomaterials are leading to new therapeutic options for a wide range of inherited and acquired diseases. Combining conventional therapies with this emerging field is a promising strategy to treat those previously-thought untreatable diseases. Traditional Chinese medicine (TCM) has evolved for thousands of years in China and still plays an important role in human health. As part of the active ingredients of TCM, proteins and peptides have attracted long-term enthusiasm of researchers. More recently, they have been utilized in gene and cell therapy, resulting in promising novel strategies to treat both cancer and non-cancer diseases. This manuscript presents a critical review on this field, accompanied with perspectives on the challenges and new directions for future research in this emerging frontier.

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Animal Venoms have Potential to Treat Cancer

Current Topics in Medicinal Chemistry ◽

10.2174/1568026619666181221120817 ◽

2019 ◽

Vol 18 (30) ◽

pp. 2555-2566 ◽

Cited By ~ 6

Author(s):

Bhaswati Chatterjee

Keyword(s):

Cancer Therapeutics ◽

Sea Anemones ◽

Anticancer Activities ◽

Inhibition Of Proliferation ◽

Cycle Arrest ◽

Venomous Animals ◽

Anti Cancer ◽

Cancerous Cells ◽

Animal Venoms ◽

Proteins And Peptides

The resistance to chemotherapeutics by the cancerous cells has made its treatment more complicated. Animal venoms have emerged as an alternative strategy for anti-cancer therapeutics. Animal venoms are cocktails of complex bioactive chemicals mainly disulfide-rich proteins and peptides with diverse pharmacological actions. The components of venoms are specific, stable, and potent and have the ability to modify their molecular targets thus making them good therapeutics candidates. The isolation of cancer-specific components from animal venoms is one of the exciting strategies in anti-cancer research. This review highlights the identified venom peptides and proteins from different venomous animals like snakes, scorpions, spiders, bees, wasps, snails, toads, frogs and sea anemones and their anticancer activities including inhibition of proliferation of cancer cells, their invasion, cell cycle arrest, induction of apoptosis and the identification of involved signaling pathways.

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Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

Current Proteomics ◽

10.2174/1570164617666191121112319 ◽

2020 ◽

Vol 17 (3) ◽

pp. 241-254

Author(s):

Yaqiong Zhang ◽

Zhiping Jia ◽

Yunyang Liu ◽

Xinwen Zhou ◽

Yi Kong

Keyword(s):

Snake Venom ◽

Protein Families ◽

Traditional Medicines ◽

Phospholipases A2 ◽

Inhibitory Peptides ◽

Sds Page ◽

Deinagkistrodon Acutus ◽

Venom Proteins ◽

Proteins And Peptides

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.

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