Academic literature on the topic 'Venom Peptide Library'
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Journal articles on the topic "Venom Peptide Library"
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Wu, Xiangyue, Yan Chen, Hao Liu, Xiangjin Kong, Xinyao Liang, Yu Zhang, Cheng Tang, and Zhonghua Liu. "The Molecular Composition of Peptide Toxins in the Venom of Spider Lycosa coelestis as Revealed by cDNA Library and Transcriptomic Sequencing." Toxins 15, no. 2 (February 10, 2023): 143. http://dx.doi.org/10.3390/toxins15020143.
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In the so-called “struggle for existence” competition, the venomous animals developed a smart and effective strategy, envenomation, for predation and defense. Biochemical analysis revealed that animal venoms are chemical pools of proteinase, peptide toxins, and small organic molecules with various biological activities. Of them, peptide toxins are of great molecular diversity and possess the capacity to modulate the activity of ion channels, the second largest group of drug targets expressed on the cell membrane, which makes them a rich resource for developing peptide drug pioneers. The spider Lycosa coelestis (L. coelestis) commonly found in farmland in China is a dominant natural enemy of agricultural pests; however, its venom composition and activity were never explored. Herein, we conducted cDNA library and transcriptomic sequencing of the venom gland of L. coelestis, which identified 1131 high-quality expressed sequence tags (ESTs), grouped into three categories denoted as toxin-like ESTs (597, 52.79%), cellular component ESTs (357, 31.56%), and non-matched ESTs (177, 15.65%). These toxin-like ESTs encode 98 non-reductant toxins, which are artificially divided into 11 families based on their sequence homology and cysteine frameworks (2–14 cysteines forming 1–7 disulfide bonds to stabilize the toxin structure). Furthermore, RP-HPLC purification combined with off-line MALDI-TOF analysis have detected 147 different peptides physically existing in the venom of L. coelestis. Electrophysiology analysis confirmed that the venom preferably inhibits the voltage-gated calcium channels in rat dorsal root ganglion neurons. Altogether, the present study has added a great lot of new members to the spider toxin superfamily and built the foundation for characterizing novel active peptides in the L. coelestis venom.
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Liao, Qingyi, Xiangjin Kong, Guoqing Luo, Xiangyue Wu, Yinping Li, Qicai Liu, Cheng Tang, and Zhonghua Liu. "Molecular Diversity of Peptide Toxins in the Venom of Spider Heteropoda pingtungensis as Revealed by cDNA Library and Transcriptome Sequencing Analysis." Toxins 14, no. 2 (February 14, 2022): 140. http://dx.doi.org/10.3390/toxins14020140.
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The venoms of toxic animals are chemical pools composed of various proteins, peptides, and small organic molecules used for predation and defense, in which the peptidic toxins have been intensively pursued mining modulators targeting disease-related ion channels and receptors as valuable drug pioneers. In the present study, we uncovered the molecular diversity of peptide toxins in the venom of the spider Heteropoda pingtungensis (H. pingtungensis) by using a combinatory strategy of venom gland cDNA library and transcriptome sequencing (RNA-seq). An amount of 991 high-quality expressed sequence tags (ESTs) were identified from 1138 generated sequences, which fall into three categories, such as the toxin-like ESTs (531, 53.58%), the cellular component ESTs (255, 25.73%), and the no-match ESTs (205, 20.69%), as determined by gene function annotations. Of them, 190 non-redundant toxin-like peptides were identified and can be artificially grouped into 13 families based on their sequence homology and cysteine frameworks (families A–M). The predicted mature toxins contain 2–10 cysteines, which are predicted to form intramolecular disulfide bonds to stabilize their three-dimensional structures. Bioinformatics analysis showed that toxins from H. pingtungensis venom have high sequences variability and the biological targets for most toxins are unpredictable due to lack of homology to toxins with known functions in the database. Furthermore, RP-HPLC and MALDI-TOF analyses have identified a total of 110 different peptides physically existing in the H. pingtungensis venom, and many RP-HPLC fractions showed potent inhibitory activity on the heterologously expressed NaV1.7 channel. Most importantly, two novel NaV1.7 peptide antagonists, µ-Sparatoxin-Hp1 and µ-Sparatoxin-Hp2, were characterized. In conclusion, the present study has added many new members to the spider toxin superfamily and built the foundation for identifying novel modulators targeting ion channels in the H. pingtungensis venom.
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Shi, Wanxia, Pengchen He, Xian-Chun Zeng, Weiwei Wu, and Xiaoming Chen. "Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the Scorpion Mesobuthus martensii Karsch." Molecules 23, no. 12 (December 14, 2018): 3314. http://dx.doi.org/10.3390/molecules23123314.
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Highly acidic peptides with no disulfide bridges are widely present in the scorpion venoms; however, none of them has been functionally characterized so far. Here, we cloned the full-length cDNA of a short-chain highly acidic peptide (referred to as HAP-1) from a cDNA library made from the venom glands of the Chinese scorpion Mesobuthus martensii Karsch. HAP-1 contains 19 amino acid residues with a predicted IP value of 4.25. Acidic amino residues account for 33.3% of the total residues in the molecule of HAP-1. HAP-1 shows 76–98% identities to some scorpion venom peptides that have not yet been functionally characterized. Secondary structure prediction showed that HAP-1 contains a beta-sheet region (residues 9–17), and two coiled coil regions (residues 1–8 and 18–19) located at the N-terminal and C-terminal regions of the peptide, respectively. Antimicrobial assay showed that HAP-1 does not have any effect on the growth of the bacterium Staphylococcus aureus AB94004. However, it potently inhibits the antimicrobial activity of a 13-mer peptide from M. martensii Karsch against Staphylococcus aureus AB94004. This finding is the first characterization of the function of such highly acidic peptides from scorpions.
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Kimura, Tadashi, Seigo Ono, and Tai Kubo. "Molecular Cloning and Sequence Analysis of the cDNAs Encoding Toxin-Like Peptides from the Venom Glands of Tarantula Grammostola rosea." International Journal of Peptides 2012 (February 29, 2012): 1–10. http://dx.doi.org/10.1155/2012/731293.
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Tarantula venom glands produce a large variety of bioactive peptides. Here we present the identification of venom components obtained by sequencing clones isolated from a cDNA library prepared from the venom glands of the Chilean common tarantula, Grammostola rosea. The cDNA sequences of about 1500 clones out of 4000 clones were analyzed after selection using several criteria. Forty-eight novel toxin-like peptides (GTx1 to GTx7, and GTx-TCTP and GTx-CRISP) were predicted from the nucleotide sequences. Among these peptides, twenty-four toxins are ICK motif peptides, eleven peptides are MIT1-like peptides, and seven are ESTX-like peptides. Peptides similar to JZTX-64, aptotoxin, CRISP, or TCTP are also obtained. GTx3 series possess a cysteine framework that is conserved among vertebrate MIT1, Bv8, prokineticins, and invertebrate astakines. GTx-CRISP is the first CRISP-like protein identified from the arthropod venom. Real-time PCR revealed that the transcripts for TCTP-like peptide are expressed in both the pereopodal muscle and the venom gland. Furthermore, a unique peptide GTx7-1, whose signal and prepro sequences are essentially identical to those of HaTx1, was obtained.
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Kalogeropoulos, Konstantinos, Andreas Treschow, Ulrich auf dem Keller, Teresa Escalante, Alexandra Rucavado, José Gutiérrez, Andreas Laustsen, and Christopher Workman. "Protease Activity Profiling of Snake Venoms Using High-Throughput Peptide Screening." Toxins 11, no. 3 (March 19, 2019): 170. http://dx.doi.org/10.3390/toxins11030170.
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Snake venom metalloproteinases (SVMPs) and snake venom serine proteinases (SVSPs) are among the most abundant enzymes in many snake venoms, particularly among viperids. These proteinases are responsible for some of the clinical manifestations classically seen in viperid envenomings, including hemorrhage, necrosis, and coagulopathies. The objective of this study was to investigate the enzymatic activities of these proteins using a high-throughput peptide library to screen for the proteinase targets of the venoms of five viperid (Echis carinatus, Bothrops asper, Daboia russelii, Bitis arietans, Bitis gabonica) and one elapid (Naja nigricollis) species of high medical importance. The proteinase activities of these venoms were each tested against 360 peptide substrates, yielding 2160 activity profiles. A nonlinear regression model that accurately described the observed enzymatic activities was fitted to the experimental data, allowing for the comparison of cleavage rates across species. In this study, previously unknown protein targets of snake venom proteinases were identified, potentially implicating novel human and animal proteins that may be involved in the pathophysiology of viper envenomings. The functional relevance of these targets was further evaluated and discussed. These new findings may contribute to our understanding of the clinical manifestations and underlying biochemical mechanisms of snakebite envenoming by viperid species.
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Hu, Zhaotun, Bo Chen, Zhen Xiao, Xi Zhou, and Zhonghua Liu. "Transcriptomic Analysis of the Spider Venom Gland Reveals Venom Diversity and Species Consanguinity." Toxins 11, no. 2 (January 24, 2019): 68. http://dx.doi.org/10.3390/toxins11020068.
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Selenocosmia jiafu (S. jiafu) has been recently identified as a new species of spider in China. It lives in the same habitat as various other venomous spiders, including Chilobrachys jingzhao (C. jingzhao), Selenocosmia huwena (S. huwena), and Macrothele raveni (M. raveni). The venom from these different species of spiders exhibits some similarities and some differences in terms of their biochemical and electrophysiological properties. With the objective to illustrate the diversity in venom peptide toxins and to establish the evolutionary relationship between different spider species, we first performed transcriptomic analysis on a cDNA library from the venom gland of S. jiafu. We identified 146 novel toxin-like sequences, which were classified into eighteen different superfamilies. This transcriptome was then compared with that of C. jingzhao, which revealed that the putative toxins from both spider venoms may have originated from the same ancestor, although novel toxins evolved independently in the two species. A BLAST search and pharmacological analysis revealed that the two venoms have similar sodium channel modulation activity. This study provides insights into the venom of two closely related species of spider, which will prove useful towards understanding the structure and function of their toxins.
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Zhang, Kangran, Yang Liu, and Yezhong Tang. "Screening of TNFR1 Binding Peptides from Deinagkistrodon acutus Venom through Phage Display." Toxins 14, no. 2 (February 19, 2022): 155. http://dx.doi.org/10.3390/toxins14020155.
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The venomous species Deinagkistrodon acutus has been used as anti-inflammatory medicine in China for a long time. It has been proven to have anti-inflammatory activity, but its specific anti-inflammatory components have not yet been fully elucidated. Tumor necrosis factor receptor-1 (TNFR1), which participates in important intracellular signaling pathways, mediates apoptosis, and functions as a regulator of inflammation, is often used as the target to develop anti-inflammatory drugs. The small peptides of snake venom have the advantages of weak immunogenicity and strong activity. To obtain the specific TNFR1 binding peptides, we constructed a T7 phage library of D. acutus venom glands, and then performed biopanning against TNFR1 on the constructed library. After biopanning three times, several sequences with potential binding capacity were obtained and one 41-amino acid peptide was selected through a series of biological analyses including sequence length, solubility, and simulated affinity, named DAvp-1. After synthesis, the binding capacity of DAvp-1 and TNFR1 was verified using surface plasmon resonance technology (SPR). Conclusively, by applying phage display technology, this work depicts the successful screening of a promising peptide DAvp-1 from D. acutus venom that binds to TNFR1. Additionally, our study emphasizes the usefulness of phage display technology for studies on screening natural product components.
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Bagheri-Ziari, Sedigheh, Delavar Shahbazzadeh, Soroush Sardari, Jean-Marc Sabatier, and Kamran Pooshang Bagheri. "Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, Hemiscorpius lepturus." Molecules 26, no. 9 (April 28, 2021): 2580. http://dx.doi.org/10.3390/molecules26092580.
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Hemiscorpius lepturus scorpion stings do not induce considerable pain based on epidemiological surveys conducted in the southwest part of Iran. Accordingly, this study was aimed to identify the analgesic molecule in H. lepturus venom by analyzing a cDNA library of the scorpion venom gland looking for sequences having homology with known animal venom analgesic peptides. The analgesic molecule is a cysteine rich peptide of 55 amino acids. the synthetic peptide was deprotected and refolded. RP-HPLC, Ellman’s, and DLS assays confirmed the refolding accuracy. Circular dichroism (CD) showed helix and beta sheet contents. This peptide, called leptucin, demonstrated 95% analgesic activity at the dose of 0.48 mg/kg in hot plate assay. Leptucin at the doses of 0.32, 0.48, and 0.64 mg/kg showed 100% activity in thermal tail flick test. No hemolysis or cytotoxicity was observed at 8 and 16 μg. Histopathology evaluations indicated no hepatotoxicity, nephrotoxicity, and cardiotoxicity. We thus report that leptucin is the analgesic agent of H. lepturus venom. Regarding the high in vivo efficacy of leptucin and the fact it shows no observable toxicity, it could be suggested as a drug lead in a preclinical study of acute pain as well as the study of its mechanism of action.
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Rajesh, R. P., Jayaseelan B. Franklin, Iffath Badsha, P. Arjun, Ruchi P. Jain, M. S. Vignesh, and Rajesh R. Kannan. "Proteome Based de novo Sequencing of Novel Conotoxins from Marine Molluscivorous Cone Snail Conus amadis and Neurological Activities of Its Natural Venom in Zebrafish Model." Protein & Peptide Letters 26, no. 11 (October 24, 2019): 819–33. http://dx.doi.org/10.2174/0929866526666190614144006.
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Background: Conus amadis is a carnivorous snail found abundantly in coastal waters of India. Despite its abundance in southern coastal waters of India and the fact that most of the conotoxin act in neuronal system, research work on Conus amadis venom was not much focused. So we have made a brief study on the venom complex of Conus amadis to identify the library of novel conotoxins and to screen the natural venom for neurological function. Objective: De novo sequencing of novel conopeptides from the venom cocktail of Conus amadis and to screen its natural venom for the presence of biological activities in zebrafish model. Methods: Proteome based MALDI-TOF and LC-MS-MS analysis for identification of novel conotoxins and subsequent sequencing. Due to the complex disulfide rich nature of the venom peptides, the study also involves global chemical modification experiments of the venom extract to unambiguously determine the sequence of novel conotoxins. Biological function analysis of natural venom was tested in zebrafish model to ascertain anti-epileptic properties. Results: In this study, we have identified 19 novel conotoxins containing 1, 2 & 3 disulfides, belonging to different classes. Among them, 2 novel contryphans, 3 T-superfamily conotoxins, 2 A-superfamily conotoxins and 2 Mini M-Superfamily conotoxins were sequenced to its amino acid level from the fragmented spectrum of singly and doubly charged parent ions using de novo sequencing strategies. ama1054, a contryphan peptide toxin, possesses post translationally modified bromo tryptophan at its seventh position. Except ama1251, all the sequenced peptide toxins possess modified C-terminal amidation. Crude venom exhibited anticonvulsant properties in pentylenetetrazole-induced seizure in zebrafish larvae, which suggested anti-epileptic property of the venom cocktail. Acetylcholinesterase activity was also identified in the venom complex. Conclusion: Based on the preliminary evidence, if this study is extended further through bioassay guided purification, could possibly yield peptide toxins with anticonvulsant and other neurologically active molecules.
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Ji, Mengyao, Tengyu Zhu, Meichen Xing, Ning Luan, James Mwangi, Xiuwen Yan, Guoxiang Mo, et al. "An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B–NS3 Protease of Flaviviruses." Toxins 11, no. 10 (October 10, 2019): 584. http://dx.doi.org/10.3390/toxins11100584.
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Flaviviruses are single-stranded RNA viruses predominantly transmitted by the widely distributed Aedes mosquitoes in nature. As important human pathogens, the geographic reach of Flaviviruses and their threats to public health are increasing, but there is currently no approved specific drug for treatment. In recent years, the development of peptide antivirals has gained much attention. Natural host defense peptides which uniquely evolved to protect the hosts have been shown to have antiviral properties. In this study, we firstly collected the venom of the Alopecosa nagpag spider from Shangri-La County, Yunnan Province. A defense peptide named Av-LCTX-An1a (Antiviral-Lycotoxin-An1a) was identified from the spider venom, and its anti-dengue serotype-2 virus (DENV2) activity was verified in vitro. Moreover, a real-time fluorescence-based protease inhibition assay showed that An1a functions as a DENV2 NS2B–NS3 protease inhibitor. Furthermore, we also found that An1a restricts zika virus (ZIKV) infection by inhibiting the ZIKV NS2B–NS3 protease. Together, our findings not only demonstrate that An1a might be a candidate for anti-flavivirus drug but also indicate that spider venom is a potential resource library rich in antiviral precursor molecules.
Dissertations / Theses on the topic "Venom Peptide Library"
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Gupta, Kallol. "Mass Spectrometric Deconvolution of Libraries of Natural Peptide Toxins." Thesis, 2013. http://etd.iisc.ac.in/handle/2005/3301.
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This thesis deals with the analysis of natural peptide libraries using mass spectrometry. In the course of the study, both ribosomal and non-ribosomal classes of peptides have been investigated. Microheterogeneity, post-translational modifications (PTM), isobaric amino acids and disulfide crosslinks present critical challenges in routine mass spectral structure determination of natural peptides. These problems form the core of this thesis. Chapter 2 describes an approach where chemical derivatization, in unison with high resolution LC-MSn experiments, resulted in deconvolution of a microheterogenous peptide library of B. subtilis K1. Chapter 3 describes an approach for distinction between isobaric amino acids (Leu/Ile/Hyp), by the use of combined ETD-CID fragmentation, through characteristic side chain losses. Chapters 4-6 address a long standing problem in structure elucidation of peptide toxins; the determination of disulfide connectivity. Through the use of direct mass spectral CID fragmentation, a methodology has been proposed for determination of the S-S pairing schemes in polypeptides. Further, an algorithm DisConnect has been developed for a rapid and robust solution to the problem. This general approach is applicable to both peptides and proteins, irrespective of the size and the number of disulfide bonds present. The method has been successfully applied to a large number of peptide toxins from marine cone snails, conotoxins, synthetic foldamers and proteins. Chapter 7 describes an attempt to integrate next generation sequencing (NGS) data with mass spectrometric analysis of the crude venom. This approach couples rapidly generated cDNA sequences, with high-throughput LC-ESI-MS/MS analysis, which provides mass spectral fragmentation information. An algorithm has been developed that allows the construction of a putative conus peptide database from the NGS data, followed by a protocol that permits rapid annotation of tandem MS data. The approach is exemplified by an analysis of the peptide components present in the venom of Conus amadis, yielding 225 chemically unique sequences, with identification of more than 150 sites of PTMs.
In summary, this thesis presents different methodologies that address the existing limitations of de novo mass spectral structure determination of natural peptides and presents new methodologies that permit for rapid and efficient analysis of complex mixtures.
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Gupta, Kallol. "Mass Spectrometric Deconvolution of Libraries of Natural Peptide Toxins." Thesis, 2013. http://etd.iisc.ernet.in/2005/3301.
Full textAbstract:
This thesis deals with the analysis of natural peptide libraries using mass spectrometry. In the course of the study, both ribosomal and non-ribosomal classes of peptides have been investigated. Microheterogeneity, post-translational modifications (PTM), isobaric amino acids and disulfide crosslinks present critical challenges in routine mass spectral structure determination of natural peptides. These problems form the core of this thesis. Chapter 2 describes an approach where chemical derivatization, in unison with high resolution LC-MSn experiments, resulted in deconvolution of a microheterogenous peptide library of B. subtilis K1. Chapter 3 describes an approach for distinction between isobaric amino acids (Leu/Ile/Hyp), by the use of combined ETD-CID fragmentation, through characteristic side chain losses. Chapters 4-6 address a long standing problem in structure elucidation of peptide toxins; the determination of disulfide connectivity. Through the use of direct mass spectral CID fragmentation, a methodology has been proposed for determination of the S-S pairing schemes in polypeptides. Further, an algorithm DisConnect has been developed for a rapid and robust solution to the problem. This general approach is applicable to both peptides and proteins, irrespective of the size and the number of disulfide bonds present. The method has been successfully applied to a large number of peptide toxins from marine cone snails, conotoxins, synthetic foldamers and proteins. Chapter 7 describes an attempt to integrate next generation sequencing (NGS) data with mass spectrometric analysis of the crude venom. This approach couples rapidly generated cDNA sequences, with high-throughput LC-ESI-MS/MS analysis, which provides mass spectral fragmentation information. An algorithm has been developed that allows the construction of a putative conus peptide database from the NGS data, followed by a protocol that permits rapid annotation of tandem MS data. The approach is exemplified by an analysis of the peptide components present in the venom of Conus amadis, yielding 225 chemically unique sequences, with identification of more than 150 sites of PTMs.
In summary, this thesis presents different methodologies that address the existing limitations of de novo mass spectral structure determination of natural peptides and presents new methodologies that permit for rapid and efficient analysis of complex mixtures.
Conference papers on the topic "Venom Peptide Library"
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Kaida, S., T. Miyata, S. Kawabata, T. Morita, Y. Yoshizawa, H. Igarashi, and S. Iwanaga. "NUCLEOTIDE SEQUENCE OF THE STAPHYLOCOAGULASE GENE FROM STAPHYLOCOCCUS AUREUS STRAIN BB." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644607.
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Staphylocoagulase (SC) is a secretary protein produced by several strains of Staphylococcus aureus (S. aureus). This protein forms a molecular complex ("staphylothrombin") with human prothrombin in a molar ratio of 1:1. The complex displays the ability to clot fibrinogen and to hydrolyze the synthetic tripeptide substrates for α-thrombin. The formation of staphylothrombin does not require proteolytic cleavage of the prothrombin molecule, and this mechanism differs markedly from the activation process by either blood-clotting factor Xa or snake venom procoagulant.In the present studies, a pAT153 library containing partial Mbo I-digested DNA prepared from aureus strain BB has been screened with a fibrin gel formation method. The identity of these clones with SC was confirmed by DNA sequence analysis and by comparison of the derived amino acid sequence with that determined for the purified SC protein. One of the positive colonies was isolated and 3.1 Kb of the insert DNA was determined by the dideoxy chain termination method. The results indicated that the insert DNA consists of 148 bp 5' flanking region, protein coding region of 715 amino acids and 746 bp 3' flanking region, and that SC from strain BB is synthesized as a precursor with a signal peptide of 26 amino acids. Thus, the mature form was composed of 689 amino acids with a molecular weight of 77,337- The NH2-terminal sequence (324 amino acids) of SC isolated from S. aureus strain 213 (S. Kawabata et al. (1986): J. Biol. Chem. 261, 527-531) was compared with that of SC derived from strain BB. The sequence homology between them was found to show 57 %. It was also found that SC derived from strain BB was composed of 8 tandem repeats (27 amino acid residues in length) in the COOH-terminal region, although their functions are not known.
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Luna, Hélder Silva e., and GIULIA GRAVA. "PEPTÍDEOS ANTIVIRAIS DA PEÇONHA DE ESCORPIÃO COMO POTENCIAL FÁRMACO NO COMBATE A COVID-19: A BIOINFORMÁTICA NO DESENVOLVIMENTO DE MEDICAMENTOS." In III Congresso Brasileiro de Ciências Biologicas. Revista Multidisciplinar de Educação e Meio Ambiente, 2022. http://dx.doi.org/10.51189/iii-conbracib/7532.
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Introdução: Com relação ao vírus da Covid-19 mesmo com o desenvolvimento das vacinais e considerável aceitação das mesmas pela população, é necessária a exploração de novas tecnologias para o combate do vírus SARS-CoV-2. Alguns estudos mostram o potencial de agentes bioquímicos com origens distintas para a inibição do receptor específico desse patógeno. A proteína Spike da Covid-19 interage com a ACE2 (enzima conversora responsável por resultar a adesão do vírus no hospedeiro) iniciando o processo de infecção. Nesta sequência foram desenvolvidos trabalhos que ressaltam a importância dos peptídeos antivirais (AVP´s) de origem natural. Para estes estudos, o emprego da bioinformática contribui para possíveis desenvolvimentos de medicamentos. Objetivo: Neste contexto o objetivo do estudo foi pesquisar os peptídeos com potencial antiviral presentes na peçonha de algumas espécies de escorpiões através de análises computacionais. Metodologia: Foi realizada uma revisão de literatura acessando os seguintes bancos de dados: Scientific Eletronic Library Online (SciELO); National Library of Medicine National Institute of Health (PubMed) e Literatura Latino-Americana e do Caribe em Ciências da Saúde (Lilacs) com os descritores: “Scorpion” “Venom” “Covid-19”. Resultados: Foram encontradas seis publicações e destas selecionadas uma, aplicando o critério de inclusão: o uso de AVP´s do veneno do escorpião no combate a Covid-19 associados a estudos de bioinformática. Os critérios de exclusão foram: pesquisas que não estivessem relacionadas ao tema específico proposto assim como artigos duplicados. Como resultados observou-se nas modelagens e simulações que o peptídeo Meucina-18 altera a conformação nativa do domínio de ligação do receptor (RBD) da proteína Spike e leva a interação incorreta do RDB com o receptor ACE2 e a sua mutação A9T que impede a interação do domínio RDB com o receptor ACE2. Conclusão: O potencial das AVP´s da peçonha de escorpião no combate de viroses associados às tecnologias de modelagens e simulações biológicas, pela bioinformática, são muito promissores para o desenvolvimento de novos medicamentos extraídos de toxinas biológicas.