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Revisiting the insights and applications of protein engineered hydrogels.
J, B, Chanda, K, M M, B
Materials science & engineering. C, Materials for biological applications. 2019;:312-327
Abstract
Utilization of protein-protein interactions or protein-peptide interactions has led to new crosslinking chemistries, resulting into protein hydrogels. Enzyme catalyzed crosslinking of specific amino acids has also been used to generate crosslinked protein hydrogels. Weak, temporary, reversible or non-covalently crosslinked protein gels as well as strong, permanent, irreversible or covalently crosslinked protein gels with mechanical strengths of varying degrees are generated by means of various crosslinking strategies. These protein hydrogels are tailored by means of protein engineering and recombinant DNA technology, depending on its end use as scaffolds for specific tissue engineering, drug delivery, wound dressings etc. This review aims to cover the advancements in the use of protein engineering along with different crosslinking techniques to create novel protein hydrogels that finds various applications in biomedical industries.
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Current state of art after twenty years of the discovery of bioactive peptide lunasin.
Fernández-Tomé, S, Hernández-Ledesma, B
Food research international (Ottawa, Ont.). 2019;:71-78
Abstract
Non-communicable diseases have become the medical challenge of the 21st century because of their high incidence and mortality rates. Accumulating evidence has suggested that the modulation of diet and other lifestyle habits is the best strategy for the prevention of these diseases. An increasing number of dietary compounds have been found to exert health promoting benefits beyond their nutritional effects. Among them, lunasin is considered one of the most studied bioactive peptides. Since its discovery in soybean twenty years ago, many researchers around the world have focused their studies on demonstrating the chemopreventive and chemotherapeutic activity of lunasin. Moreover, in the last years, promising protective effects of this peptide against hypercholesterolemia, obesity, metabolic syndrome and associated cardiovascular disorders, and inflammatory and immune-regulated diseases have been described. This review summarizes recent remarkable advances on the use of peptide lunasin as a potential functional ingredient to provide health benefits. Moreover, novel aspects related to the influence of lunasin's digestion and bioavailability, the mechanisms of action proposed to explain the underlying biological properties, and the incorporation of this peptide into nutritional supplements are critically discussed.
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3.
Bioactive peptides from selected latin american food crops - A nutraceutical and molecular approach.
Orona-Tamayo, D, Valverde, ME, Paredes-López, O
Critical reviews in food science and nutrition. 2019;(12):1949-1975
Abstract
This review reported an updated survey on the molecular functional properties of bioactive peptides derived from different Latin American ancient grains such as Maize, common Bean, Amaranth, Quinoa and Chia seeds. Seed storage proteins ecrypt in their sequences diverse peptides associated with a wide range of beneficial effects on the human health and the most studied are antihypertensive, anti-cholesterolemic, antioxidant, anti-inflammatory, anticancer, antimicrobial and immunomodulatory properties. Additionally, in the last decades molecular properties have been also used for their characterization to understand their activities and it makes them highly attractive to be incorporated into food formulations and to complement or replace some conventional cereal grains. Due to the nutraceutical effects, today, these seeds are one of the main gastronomic trends of consumption worldwide due to their nutritional benefits and are part of the shopping lists of many people, among them vegetarians, vegans, celiacs or lovers of raw food. These seeds are a legacy of pre-Columbian civilizations reason why in our time they are considered as "Superfoods of the Gods", "The pre-hispanic superfoods of the future" and "The new golden seeds of the XXI century".
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4.
Proline-containing peptides-New insight and implications: A Review.
Misiura, M, Miltyk, W
BioFactors (Oxford, England). 2019;(6):857-866
Abstract
The family of regulatory proline-containing peptides (PCPs), also known as glyprolines, exhibit significant biological activity. The group of glyprolines includes Gly-Pro (GP), Pro-Gly-Pro (PGP), cyclic Gly-Pro (cGP), as well as PGP derivatives, for example, N-acetylated PGP (N-a-PGP) and N-methylated PGP (N-m-PGP). PCPs are engaged in various biological processes including the proinflammatory neutrophil chemoattraction in lung diseases, inflammatory bowel diseases or ischemic stroke. Glyprolines have been also postulated to play an important role as atheroprotective and anticoagulant agents, exhibit neuroprotective effects in Parkinson's disease, as well as regulate insulin-like growth factor (IGF) homeostasis. It was also noticed that PCPs inhibit proliferation and migration of keratinocytes in wound healing, protection of the gastric mucosa and stimulation of its regeneration. The regulatory glyprolines are derived from endogenous and exogenous sources. Most PCPs are derived from collagen or diet protein degradation. Recently, great interest is concentrated on short proline-rich oligopeptides derived from IGF-1 degradation. The mechanism of PCPs biological activity is not fully explained. It involves receptor-mediated mechanisms, for example, N-a-PGP acts as CXCR1/2 receptor ligand, whereas cGP regulates IGF-1 bioavailability by modifying the IGF-1 binding to the IGF-1 binding protein-3. PGP has been observed to interact with collagen-specific receptors. The data suggest a promising role of PGP as a target of various diseases therapy. This review is focused on the effect of PCPs on metabolic processes in different tissues and the molecular mechanism of their action as an approach to pharmacotherapy of PCPs-dependent diseases.
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5.
Anticancer Activities of Natural and Synthetic Peptides.
Hilchie, AL, Hoskin, DW, Power Coombs, MR
Advances in experimental medicine and biology. 2019;:131-147
Abstract
Anticancer peptides (ACPs) are cationic amphipathic peptides that bind to and kill cancer cells either by a direct- or indirect-acting mechanism. ACPs provide a novel treatment strategy, and selected ACPs are currently in phase I clinical trials to examine their safety and overall benefit in cancer patients. Increasing the selectivity of ACPs is important so that these peptides kill cancer cells without harming normal cells. Peptide sequence modifications may help to improve ACP selectivity. ACPs also have immune-modulatory effects, including the release of danger signals from dying cancer cells, induction of chemokine genes, increasing T-cell immune responses, and inhibiting T regulatory cells. These effects ultimately increase the potential for an effective anticancer immune response that may contribute to long-term benefits and increased patient survival. Packaging ACPs in nanoparticles or fusogenic liposomes may be beneficial for increasing ACP half-life and enhancing the delivery of ACPs to tumor target cells. Additionally, engineering ACP-producing oncolytic viruses may be an effective future treatment strategy. Overall research in this area has been slow to progress, but with ongoing ACP-based clinical trials, the potential for ACPs in cancer treatments is closer to being realized. The integration of basic research with computer modeling of ACPs is predicted to substantially advance this field of research.
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6.
Polyglutamine Repeats in Viruses.
Schein, CH
Molecular neurobiology. 2019;(5):3664-3675
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Abstract
This review explores the presence and functions of polyglutamine (polyQ) in viral proteins. In mammals, mutations in polyQ segments (and CAG repeats at the nucleotide level) have been linked to neural disorders and ataxias. PolyQ regions in normal human proteins have documented functional roles, in transcription factors and, more recently, in regulating autophagy. Despite the high frequency of polyQ repeats in eukaryotic genomes, little attention has been given to the presence or possible role of polyQ sequences in virus genomes. A survey described here revealed that polyQ repeats occur rarely in RNA viruses, suggesting that they have detrimental effects on virus replication at the nucleotide or protein level. However, there have been sporadic reports of polyQ segments in potyviruses and in reptilian nidoviruses (among the largest RNA viruses known). Conserved polyQ segments are found in the regulatory control proteins of many DNA viruses. Variable length polyQ tracts are found in proteins that contribute to transmissibility (cowpox A-type inclusion protein (ATI)) and control of latency (herpes viruses). New longer-read sequencing methods, using original biological samples, should reveal more details on the presence and functional role of polyQ in viruses, as well as the nucleotide regions that encode them. Given the known toxic effects of polyQ repeats, the role of these segments in neurovirulent and tumorigenic viruses should be further explored.
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7.
Small open reading frames and cellular stress responses.
Khitun, A, Ness, TJ, Slavoff, SA
Molecular omics. 2019;(2):108-116
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Abstract
Small open reading frames (smORFs) encoding polypeptides of less than 100 amino acids in eukaryotes (50 amino acids in prokaryotes) were historically excluded from genome annotation. However, recent advances in genomics, ribosome footprinting, and proteomics have revealed thousands of translated smORFs in genomes spanning evolutionary space. These smORFs can encode functional polypeptides, or act as cis-translational regulators. Herein we review evidence that some smORF-encoded polypeptides (SEPs) participate in stress responses in both prokaryotes and eukaryotes, and that some upstream ORFs (uORFs) regulate stress-responsive translation of downstream cistrons in eukaryotic cells. These studies provide insight into a regulated subclass of smORFs and suggest that at least some SEPs may participate in maintenance of cellular homeostasis under stress.
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8.
Adenylation Domains in Nonribosomal Peptide Engineering.
Stanišić, A, Kries, H
Chembiochem : a European journal of chemical biology. 2019;(11):1347-1356
Abstract
Nonribosomal peptides are a prolific source of bioactive molecules biosynthesized on large, modular assembly line synthetases. Synthetic biologists seek to obtain tailored peptides with tuned or novel bioactivities by engineering modules and domains of these nonribosomal peptide synthetases. The activation step catalyzed by adenylation domains primarily selects which amino acids are incorporated into nonribosomal peptides. Here, we review experimental protocols for probing the adenylation reaction that are applicable in natural product discovery and engineering. Several alternatives to the established pyrophosphate exchange assay will be compared and potential pitfalls pointed out. Binding pocket mutagenesis of adenylation domains has been successfully conducted to adjust substrate preferences. Novel screening methods relying on yeast surface display, for instance, search a larger sequence space for improved mutants and thus allow more substantial changes in peptide structure.
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Med15: Glutamine-Rich Mediator Subunit with Potential for Plasticity.
Cooper, DG, Fassler, JS
Trends in biochemical sciences. 2019;(9):737-751
Abstract
The Mediator complex is required for basal activity of the RNA polymerase (Pol) II transcriptional apparatus and for responsiveness to some activator proteins. Med15, situated in the Mediator tail, plays a role in transmitting regulatory information from distant DNA-bound transcription factors to the transcriptional apparatus poised at promoters. Yeast Med15 and its orthologs share an unusual, glutamine-rich amino acid composition. Here, we discuss this sequence feature and the tendency of polyglutamine tracts to vary in length among strains of Saccharomyces cerevisiae, and we propose that different polyglutamine tract lengths may be adaptive within certain domestication habitats.
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10.
Hypoallergenic Proteins for the Treatment of Food Allergy.
Yang, L, Kulis, M
Current allergy and asthma reports. 2019;(2):15
Abstract
PURPOSE OF REVIEW Food allergy is a growing health problem worldwide that impacts millions of individuals. Current treatment options are limited and strict dietary avoidance remains the standard of care. Immunotherapy using whole, native allergens is under active clinical investigation but harbors the risk of severe side effects including anaphylaxis. Newer food-specific therapies with hypoallergenic proteins may potentially offer safer treatment alternatives, and this review seeks to investigate the evidence supporting the use of these modalities. RECENT FINDINGS The utilization of different methods to alter allergen structure and IgE binding leads to reduced allergenicity and decreases the risk for systemic reactions, making the use of potential therapies including extensively heated egg/milk, peptide immunotherapy, recombinant allergen immunotherapy, and DNA vaccines safe and possibly efficacious forms of treatment in food allergy. However, for the majority of these treatment modalities, limited data currently exists looking at the safety and efficacy in human subjects with food allergy. This review provides a comprehensive overview of the current evidence examining the safety and efficacy of hypoallergenic proteins in the treatment of food allergies.