Vladimir Egorov, Natalia Grudinina, Andrey Vasin, Dmitry Lebedev
{"title":"Peptide-Induced Amyloid-Like Conformational Transitions in Proteins.","authors":"Vladimir Egorov, Natalia Grudinina, Andrey Vasin, Dmitry Lebedev","doi":"10.1155/2015/723186","DOIUrl":"https://doi.org/10.1155/2015/723186","url":null,"abstract":"<p><p>Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2015 ","pages":"723186"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2015/723186","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34231282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cationic Bioactive Peptide from the Seeds of Benincasa hispida.","authors":"Sunayana Sharma, Hirday Narain Verma, Nilesh Kumar Sharma","doi":"10.1155/2014/156060","DOIUrl":"https://doi.org/10.1155/2014/156060","url":null,"abstract":"<p><p>A designated bioactive peptide \"Hispidalin\" purified from the seeds of Benincasa hispida, which is a medicinal plant, belongs to Cucurbitaceae family. Purification was achieved by using a procedure consisting of extraction from potassium phosphate buffer followed by FPLC and HPLC steps. Based on amino acid residue, this peptide is amphipathic and basic with one net positive charge having isoelectric pH 8.1. This peptide is without sulphur containing amino acid suggesting its extended conformation lacking double bond secondary structure. The results obtained from MALDI-TOF suggested that Hispidalin is of molecular mass 5.7 KDa with 49 amino acid residues and confirmed SDS-PAGE resolved ∼ 6.0 KDa protein band. This novel and unknown peptide \"Hispidalin\" showed broad and potent inhibitory effects against various human bacterial and fungal pathogens; its growth inhibition was significantly comparable with commercial antibacterial and antifungal drugs. The Hispidalin at 40 μ g/mL concentration exhibited 70.8% DPPH free radical-scavenging activity and 69.5% lipid peroxide inhibition. Thus, in the present study, Hispidalin demonstrated remarkable antimicrobial and antioxidant potentials from the seeds of B. hispida. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2014 ","pages":"156060"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2014/156060","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32347367","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Epithelial antimicrobial peptides: guardian of the oral cavity.","authors":"Mayank Hans, Veenu Madaan Hans","doi":"10.1155/2014/370297","DOIUrl":"https://doi.org/10.1155/2014/370297","url":null,"abstract":"<p><p>Gingival epithelium provides first line of defence from the microorganisms present in dental plaque. It not only provides a mechanical barrier but also has an active immune function too. Gingival epithelial cells participate in innate immunity by producing a range of antimicrobial peptides to protect the host against oral pathogens. These epithelial antimicrobial peptides (EAPs) include the β-defensin family, cathelicidin (LL-37), calprotectin, and adrenomedullin. While some are constitutively expressed in gingival epithelial cells, others are induced upon exposure to microbial insults. It is likely that these EAPs have a role in determining the initiation and progression of oral diseases. EAPs are broad spectrum antimicrobials with a different but overlapping range of activity. Apart from antimicrobial activity, they participate in several other crucial roles in host tissues. Some of these, for instance, β-defensins, are chemotactic to immune cells. Others, such as calprotectin are important for wound healing and cell proliferation. Adrenomedullin, a multifunctional peptide, has its biological action in a wide range of tissues. Not only is it a potent vasodilator but also it has several endocrine effects. Knowing in detail the various bioactions of these EAPs may provide us with useful information regarding their utility as therapeutic agents. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2014 ","pages":"370297"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2014/370297","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32847085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lei Shi, Pang-Hu Zhou, Juan-Li Xi, Hong-Gang Yu, Bing-Hong Zhang
{"title":"Recombinant human trefoil factor 3 ameliorates bowel injury: its anti-inflammatory effect on experimental necrotizing enterocolitis.","authors":"Lei Shi, Pang-Hu Zhou, Juan-Li Xi, Hong-Gang Yu, Bing-Hong Zhang","doi":"10.1155/2014/634135","DOIUrl":"https://doi.org/10.1155/2014/634135","url":null,"abstract":"<p><p>Aim. Recombinant human trefoil factor 3 (intestinal trefoil factor) has been suggested to be partially protective against necrotizing enterocolitis (NEC), but the mechanisms of this protection have not been defined. We investigated whether the protective effects of rhTFF3 are the result of an anti-inflammatory response. Methods. The rats were killed on day 4, the distal ileum was harvested for morphological studies and immunohistochemistry for NF- κ B (p65), and the amounts of IL-1 β , IL-6, and IL-10 in the intestinal tissue were measured using commercial ELISA assay kits. Results. In the neonatal NEC, IL-1 β , IL-6, and IL-10 were significantly higher than in normal group. In normal group, IL-1 β and IL-6 were significantly decreased, and the amount of IL-10 was markedly increased compared with NEC group. In the NEC model, immunohistochemical staining for NF- κ B (p65) was demonstrated to be of a strong brown color and was distributed in the intestinal epithelium. Treatment with rhTFF3 significantly decreased the immunoreactivity of NF- κ B (p65) in the NEC model. Conclusions. Intestinal inflammation was ameliorated after rhTFF3 was injected. rhTFF3 may protect against the intestinal injury of the neonatal rat NEC model by suppression of the inflammatory response. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2014 ","pages":"634135"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2014/634135","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32223800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Sequence Determination of a Novel Tripeptide Isolated from the Young Leaves of Azadirachta indica A. Juss.","authors":"M Rajeswari Prabha, B Ramachandramurty","doi":"10.1155/2013/629549","DOIUrl":"https://doi.org/10.1155/2013/629549","url":null,"abstract":"<p><p>The neem tree has long been recognized for its unique properties, both against insects and in improving human health. Every part of the tree has been used as a traditional medicine for household remedy against various human ailments, from antiquity. Although the occurrence of various phytochemicals in neem has been studied, we have identified the presence of a novel tripeptide in the young leaves of neem using a simple and inexpensive paper chromatographic method, detected by Cu(II)-ninhydrin reagent. The peptide nature of the isolated compound is confirmed by spectral studies. The sequence of the peptide is determined using de novo sequencing by tandem MS after purification.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2013 ","pages":"629549"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/629549","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31319495","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Antimicrobial peptides: versatile biological properties.","authors":"Muthuirulan Pushpanathan, Paramasamy Gunasekaran, Jeyaprakash Rajendhran","doi":"10.1155/2013/675391","DOIUrl":"https://doi.org/10.1155/2013/675391","url":null,"abstract":"<p><p>Antimicrobial peptides are diverse group of biologically active molecules with multidimensional properties. In recent past, a wide variety of AMPs with diverse structures have been reported from different sources such as plants, animals, mammals, and microorganisms. The presence of unusual amino acids and structural motifs in AMPs confers unique structural properties to the peptide that attribute for their specific mode of action. The ability of these active AMPs to act as multifunctional effector molecules such as signalling molecule, immune modulators, mitogen, antitumor, and contraceptive agent makes it an interesting candidate to study every aspect of their structural and biological properties for prophylactic and therapeutic applications. In addition, easy cloning and recombinant expression of AMPs in heterologous plant host systems provided a pipeline for production of disease resistant transgenic plants. Besides these properties, AMPs were also used as drug delivery vectors to deliver cell impermeable drugs to cell interior. The present review focuses on the diversity and broad spectrum antimicrobial activity of AMPs along with its multidimensional properties that could be exploited for the application of these bioactive peptides as a potential and promising drug candidate in pharmaceutical industries. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2013 ","pages":"675391"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/675391","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31648929","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Marina de Oliveira Paro, Cyntia Silva Ferreira, Fernanda Silva Vieira, Marcos Aurélio de Santana, William Castro-Borges, Maria Sueli Silva Namen-Lopes, Sophie Yvette Leclercq, Cibele Velloso-Rodrigues, Milton Hércules Guerra de Andrade
{"title":"Antigenic Peptides Capable of Inducing Specific Antibodies for Detection of the Major Alterations Found in Type 2B Von Willebrand Disease.","authors":"Marina de Oliveira Paro, Cyntia Silva Ferreira, Fernanda Silva Vieira, Marcos Aurélio de Santana, William Castro-Borges, Maria Sueli Silva Namen-Lopes, Sophie Yvette Leclercq, Cibele Velloso-Rodrigues, Milton Hércules Guerra de Andrade","doi":"10.1155/2013/590329","DOIUrl":"https://doi.org/10.1155/2013/590329","url":null,"abstract":"<p><p>Von Willebrand disease (VWD) is an inherited hemorrhagic disorder promoted by either quantitative or qualitative defects of the von Willebrand factor (VWF). The disease represents the most common human coagulopathy afflicting 1.3% of the population. Qualitative defects are subdivided into four subtypes and classified according to the molecular dysfunction of the VWF. The differential diagnosis of the VWD is a difficult task, relying on a panel of tests aimed to assess the plasma levels and function of the VWF. Here, we propose biochemical approaches for the identification of structural variants of the VWF. A bioinformatic analysis was conducted to design seven peptides among which three were representatives of specific amino acid sequences belonging to normal VWF and four encompassed sequences found in the most common VWD subtype 2B. These peptides were used to immunize mice, after which, peptide-specific immunoglobulins were purified. This resulted in four Ig preparations capable of detecting alterations in the subtype 2B VWD plus additional three antibody fractions targeting the normal VWF. The panel of antibodies could serve many applications among them (1) assessment of VWF: antigen interaction, (2) VWF multimer analysis, and (3) production of monoclonal antibodies against VWF for therapeutic purposes as in thrombotic thrombocytopenic purpura. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2013 ","pages":"590329"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/590329","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31678745","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Maria Cristina Vianna Braga, Arthur Andrade Nery, Henning Ulrich, Katsuhiro Konno, Juliana Mozer Sciani, Daniel Carvalho Pimenta
{"title":"α -RgIB: A Novel Antagonist Peptide of Neuronal Acetylcholine Receptor Isolated from Conus regius Venom.","authors":"Maria Cristina Vianna Braga, Arthur Andrade Nery, Henning Ulrich, Katsuhiro Konno, Juliana Mozer Sciani, Daniel Carvalho Pimenta","doi":"10.1155/2013/543028","DOIUrl":"https://doi.org/10.1155/2013/543028","url":null,"abstract":"<p><p>Conus venoms are rich sources of biologically active peptides that act specifically on ionic channels and metabotropic receptors present at the neuromuscular junction, efficiently paralyzing the prey. Each species of Conus may have 50 to 200 uncharacterized bioactive peptides with pharmacological interest. Conus regius is a vermivorous species that inhabits Northeastern Brazilian tropical waters. In this work, we characterized one peptide with activity on neuronal acetylcholine receptor (nAChR). Crude venom was purified by reverse-phase HPLC and selected fractions were screened and sequenced by mass spectrometry, MALDI-ToF, and ESI-Q-ToF, respectively. A new peptide was identified, bearing two disulfide bridges. The novel 2,701 Da peptide belongs to the cysteine framework I, corresponding to the cysteine pattern CC-C-C. The biological activity of the purified peptide was tested by intracranial injection in mice, and it was observed that high concentrations induced hyperactivity in the animals, whereas lower doses caused breathing difficulty. The activity of this peptide was assayed in patch-clamp experiments, on nAChR-rich cells, in whole-cell configuration. The peptide blocked slow rise-time neuronal receptors, probably α 3 β 4 and/or α 3 β 4 α 5 subtype. According to the nomenclature, the new peptide was designated as α -RgIB.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":" ","pages":"543028"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/543028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40229273","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Significant increase in salivary substance p level after a single oral dose of cevimeline in humans.","authors":"Yosuke Suzuki, Hiroki Itoh, Kohei Amada, Ryota Yamamura, Yuhki Sato, Masaharu Takeyama","doi":"10.1155/2013/284765","DOIUrl":"https://doi.org/10.1155/2013/284765","url":null,"abstract":"<p><p>Cevimeline is a novel muscarinic acetylcholine receptor agonist currently being developed as a therapeutic agent for xerostomia. We examined the effects of cevimeline on salivary and plasma levels of substance-P- (SP-), calcitonin-gene-related-peptide- (CGRP-), and vasoactive-intestinal-polypeptide- (VIP-) like immunoreactive substances (ISs) in humans. An open-labeled crossover study was conducted on seven healthy volunteers. Saliva volume was measured, and saliva and venous blood samples were collected before and 30-240 min after a single oral dose of cevimeline or placebo. Salivary and plasma levels of SP-, CGRP-, and VIP-IS were measured using a highly sensitive enzyme immunoassay. A single oral dose of cevimeline resulted in significant increases in salivary but not plasma SP-IS level compared to placebo. Cevimeline administration did not alter the salivary or plasma levels of CGRP-IS or VIP-IS compared to placebo. Significant increases in salivary volume were observed after cevimeline administration compared to placebo. A significant correlation was observed between the total release of SP-IS and that of salivary volume. These findings suggest an association of SP with the enhancement of salivary secretion by cevimeline.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2013 ","pages":"284765"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/284765","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31360294","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Vincent C H Lee, Elizabeth N Lloyd, Helena C Dearden, Kenneth Wong
{"title":"A systematic review to investigate whether Angiotensin-(1-7) is a promising therapeutic target in human heart failure.","authors":"Vincent C H Lee, Elizabeth N Lloyd, Helena C Dearden, Kenneth Wong","doi":"10.1155/2013/260346","DOIUrl":"https://doi.org/10.1155/2013/260346","url":null,"abstract":"<p><p>Context. Heart failure (HF) is a common condition causing much morbidity and mortality despite major advances in pharmacological and device therapies. Preclinical data suggest a cardioprotective role of Angiotensin-(1-7) in animal models of HF. Objective. Perform a systematic review on the effects of Angiotensin-(1-7) on humans, focusing on HF. Results. 39 studies were included in the review (4 in human HF and (35) in non-HF patients). There is only one intervention study on 8 patients with human HF, using Angiotensin-(1-7), with forearm blood flow (FBF) as the endpoint. Angiotensin-(1-7) caused no significant effect on FBF in this HF study but caused vasodilation in 3 out of 4 non-HF studies. In one other non-HF study, Angiotensin-(1-7) infusion led to a significant increase in blood pressure in normal men; however, effects were <0.03% that of angiotensin II. Cardioprotective effects seen in non-HF studies include for instance beneficial actions against atherosclerosis and myocardial fibrosis. Conclusions. The main finding of our systematic review is that Angiotensin-(1-7) plays an important cardioprotective role in HF in animals and in patients without heart failure. More research is required to test the hypothesis that Angiotensin-(1-7) benefits patients with heart failure. </p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2013 ","pages":"260346"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/260346","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32055325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}