{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T07:41:15Z","timestamp":1791877275353,"version":"4.3.4"},"reference-count":44,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"National Council for Scientific and Technological Development (CNPq)"},{"DOI":"10.13039\/501100001807","name":"S\u00e3o Paulo Research Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100010072","name":"Animal Toxins Research Support Center","doi-asserted-by":"crossref","award":["NAP-TOXAN-USP"],"award-info":[{"award-number":["NAP-TOXAN-USP"]}],"id":[{"id":"10.13039\/501100010072","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Peptides"],"published-print":{"date-parts":[[2018,4]]},"DOI":"10.1016\/j.peptides.2018.01.015","type":"journal-article","created":{"date-parts":[[2018,2,2]],"date-time":"2018-02-02T01:29:46Z","timestamp":1517534986000},"page":"1-7","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":20,"special_numbering":"C","title":["LmrBPP9: A synthetic bradykinin-potentiating peptide from Lachesis muta rhombeata venom that inhibits the angiotensin-converting enzyme activity in vitro and reduces the blood pressure of hypertensive rats"],"prefix":"10.1016","volume":"102","author":[{"given":"Ernesto Lopes","family":"Pinheiro-J\u00fanior","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johara","family":"Boldrini-Fran\u00e7a","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luciana Mattoso Pires","family":"de Campos Ara\u00fajo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norival Alves","family":"Santos-Filho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lusiane Maria","family":"Bendhack","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eduardo Maffud","family":"Cilli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eliane Candiani","family":"Arantes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"11","key":"10.1016\/j.peptides.2018.01.015_bib0005","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1074\/mcp.M112.019331","article-title":"Peptidomics of three Bothrops snake venoms: insights into the molecular diversification of proteomes and peptidomes","volume":"11","author":"Tashima","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"issue":"5","key":"10.1016\/j.peptides.2018.01.015_bib0010","doi-asserted-by":"crossref","first-page":"2278","DOI":"10.1021\/pr901027r","article-title":"Analysis of the ontogenetic variation in the venom proteome\/peptidome of Bothrops jararaca reveals different strategies to deal with prey","volume":"9","author":"Zelanis","year":"2010","journal-title":"J. Proteome Res."},{"issue":"6","key":"10.1016\/j.peptides.2018.01.015_bib0015","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1111\/bjh.14591","article-title":"Haemotoxic snake venoms: their functional activity, impact on snakebite victims and pharmaceutical promise","volume":"177","author":"Slagboom","year":"2017","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.peptides.2018.01.015_bib0020","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.jprot.2013.05.028","article-title":"Snake venomics of Lachesis muta rhombeata and genus-wide antivenomics assessment of the paraspecific immunoreactivity of two antivenoms evidence the high compositional and immunological conservation across Lachesis","volume":"89","author":"Pla","year":"2013","journal-title":"J. Proteomics"},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0025","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1152\/ajplegacy.1949.156.2.261","article-title":"Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin","volume":"156","author":"Rocha","year":"1949","journal-title":"Am. J. Physiol."},{"issue":"9","key":"10.1016\/j.peptides.2018.01.015_bib0030","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1016\/j.bcp.2007.07.014","article-title":"Identification of novel bradykinin-potentiating peptides (BPPs) in the venom gland of a rattlesnake allowed the evaluation of the structure-function relationship of BPPs","volume":"74","author":"Gomes","year":"2007","journal-title":"Biochem. Pharmacol."},{"issue":"4","key":"10.1016\/j.peptides.2018.01.015_bib0035","first-page":"552","article-title":"Effects of three vasoactive peptides isolated from the plasma of the snake Bothrops jararaca, Comparative biochemistry and physiology","volume":"149","author":"Barreto","year":"2009","journal-title":"Toxicol. Pharmacol.: CBP"},{"issue":"7","key":"10.1016\/j.peptides.2018.01.015_bib0040","doi-asserted-by":"crossref","first-page":"658","DOI":"10.2174\/1568026615666150217113835","article-title":"Hypotensive peptides from snake venoms: structure, function and mechanism","volume":"15","author":"Xu","year":"2015","journal-title":"Curr. Top. Med. Chem."},{"issue":"1","key":"10.1016\/j.peptides.2018.01.015_bib0045","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.jprot.2007.10.004","article-title":"Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis","volume":"71","author":"Sanz","year":"2008","journal-title":"J. Proteomics"},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0050","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1111\/j.1476-5381.1971.tb07113.x","article-title":"Action of bradykinin potentiating factor (BPF) and dimercaprol (BAL) on the responses to bradykinin of isolated preparations of rat intestines","volume":"42","author":"Camargo","year":"1971","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.peptides.2018.01.015_bib0055","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1186\/s40409-017-0134-7","article-title":"The modular nature of bradykinin-potentiating peptides isolated from snake venoms","volume":"23","author":"Sciani","year":"2017","journal-title":"J. Venomous Anim. Toxins Incl. Trop. Dis."},{"issue":"7","key":"10.1016\/j.peptides.2018.01.015_bib0060","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.peptides.2004.04.006","article-title":"Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography","volume":"25","author":"Ianzer","year":"2004","journal-title":"Peptides"},{"issue":"4","key":"10.1016\/j.peptides.2018.01.015_bib0065","first-page":"554","article-title":"Using bradykinin-potentiating peptide structures to develop new antihypertensive drugs","volume":"3","author":"Fernandez","year":"2004","journal-title":"Genet. Mol. Res."},{"issue":"12","key":"10.1016\/j.peptides.2018.01.015_bib0070","doi-asserted-by":"crossref","first-page":"3298","DOI":"10.1039\/c1mb05309d","article-title":"Venom peptide analysis of Vipera ammodytes meridionalis (Viperinae) and Bothrops jararacussu (Crotalinae) demonstrates subfamily-specificity of the peptidome in the family Viperidae","volume":"7","author":"Munawar","year":"2011","journal-title":"Mol. Biosyst."},{"issue":"4","key":"10.1016\/j.peptides.2018.01.015_bib0075","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.biopha.2011.10.001","article-title":"Characterization of two vasoactive peptides isolated from the plasma of the snake Crotalus durissus terrificus","volume":"66","author":"Barreto","year":"2012","journal-title":"Biomed. Pharmacother."},{"issue":"4","key":"10.1016\/j.peptides.2018.01.015_bib0080","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1161\/01.HYP.17.4.589","article-title":"History of the design of captopril and related inhibitors of angiotensin converting enzyme","volume":"17","author":"Cushman","year":"1991","journal-title":"Hypertension"},{"issue":"6","key":"10.1016\/j.peptides.2018.01.015_bib0085","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1161\/CIRCULATIONAHA.115.018912","article-title":"Global disparities of hypertension prevalence and control: a systematic analysis of population-based studies from 90 countries","volume":"134","author":"Mills","year":"2016","journal-title":"Circulation"},{"issue":"10064","key":"10.1016\/j.peptides.2018.01.015_bib0090","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0140-6736(16)31919-5","article-title":"Worldwide trends in blood pressure from 1975 to 2015: a pooled analysis of 1479 population-based measurement studies with 19.1 million participants","volume":"389","author":"N.C.D.R.F. Collaboration","year":"2017","journal-title":"Lancet"},{"issue":"3","key":"10.1016\/j.peptides.2018.01.015_bib0095","first-page":"261","article-title":"Venoms, toxins and derivatives from the Brazilian fauna: valuable sources for drug discovery","volume":"67","author":"De Marco Almeida","year":"2015","journal-title":"Sheng Li Xue Bao"},{"key":"10.1016\/j.peptides.2018.01.015_bib0100","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.toxicon.2014.10.020","article-title":"Toxins and drug discovery","volume":"92","author":"Harvey","year":"2014","journal-title":"Toxicon"},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0105","doi-asserted-by":"crossref","first-page":"28","DOI":"10.4331\/wjbc.v6.i2.28","article-title":"Animal venom studies: current benefits and future developments","volume":"6","author":"Utkin","year":"2015","journal-title":"World J. Biol. Chem."},{"key":"10.1016\/j.peptides.2018.01.015_bib0110","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.toxicon.2013.03.020","article-title":"Snake venomics: from the inventory of toxins to biology","volume":"75","author":"Calvete","year":"2013","journal-title":"Toxicon"},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0115","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.jpba.2004.11.004","article-title":"Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides","volume":"37","author":"Li","year":"2005","journal-title":"J. Pharm. Biomed. Anal."},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0120","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1084\/jem.65.2.233","article-title":"Studies on experimental hypertension: Ii. The effect of resection of splanchnic nerves on experimental renal hypertension","volume":"65","author":"Goldblatt","year":"1937","journal-title":"J. Exp. Med."},{"issue":"1","key":"10.1016\/j.peptides.2018.01.015_bib0125","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.toxicon.2005.03.006","article-title":"Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom","volume":"46","author":"Soares","year":"2005","journal-title":"Toxicon"},{"issue":"22","key":"10.1016\/j.peptides.2018.01.015_bib0130","doi-asserted-by":"crossref","first-page":"10881","DOI":"10.1093\/nar\/16.22.10881","article-title":"Multiple sequence alignment with hierarchical clustering","volume":"16","author":"Corpet","year":"1988","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.peptides.2018.01.015_bib0135","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12953-016-0090-0","article-title":"Isolation and characterization of Bradykinin potentiating peptides from Agkistrodon bilineatus venom","volume":"14","author":"Munawar","year":"2016","journal-title":"Proteome Sci."},{"issue":"1","key":"10.1016\/j.peptides.2018.01.015_bib0140","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1177\/106002809603000101","article-title":"Conversions from captopril to lisinopril at a dosage ratio off 5:1 result in comparable control of hypertension","volume":"30","author":"Gill","year":"1996","journal-title":"Ann. Pharmacother."},{"key":"10.1016\/j.peptides.2018.01.015_bib0145","unstructured":"J.L.C. Cardoso, F.O.d.S. Fran\u00e7a, F.H. Wen, C.M.S.A. Malaque, V. Haddad Junior, Animais pe\u00e7onhentos no Brasil: biologia, cl\u00ednica e terap\u00eautica dos acidentes, Animais pe\u00e7onhentos no Brasil: biologia, cl\u00ednica e terap\u00eautica dos acidentes, Sarvier (2003)."},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0150","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.toxicon.2005.04.011","article-title":"Neurotoxic and myotoxic actions from Lachesis muta mutamuta (surucucu) whole venom on the mouse and chick nerve-muscle preparations","volume":"46","author":"Damico","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2018.01.015_bib0155","series-title":"Asp\u00e9ctos cl\u00ednicos do acidente laqu\u00e9tico","author":"de Souza","year":"2009"},{"key":"10.1016\/j.peptides.2018.01.015_bib0160","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.toxicon.2014.07.011","article-title":"A new structurally atypical bradykinin-potentiating peptide isolated from Crotalus durissus cascavella venom (South American rattlesnake)","volume":"90","author":"Lopes","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2018.01.015_bib0165","doi-asserted-by":"crossref","DOI":"10.5772\/52509","article-title":"Applications of snake venom proline-rich oligopeptides (Bj-PROs) in disease conditions resulting from deficient nitric oxide production","author":"Lameu","year":"2013","journal-title":"Drug Discov."},{"key":"10.1016\/j.peptides.2018.01.015_bib0170","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/srep00717","article-title":"Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides","volume":"2","author":"Masuyer","year":"2012","journal-title":"Sci. Rep."},{"issue":"6","key":"10.1016\/j.peptides.2018.01.015_bib0175","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1016\/j.bcp.2010.12.016","article-title":"Bj-PRO-5a, a natural angiotensin-converting enzyme inhibitor, promotes vasodilatation mediated by both bradykinin B 2 and M1 muscarinic acetylcholine receptors","volume":"81","author":"Morais","year":"2011","journal-title":"Biochem. Pharmacol."},{"issue":"4","key":"10.1016\/j.peptides.2018.01.015_bib0180","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.toxicon.2011.07.013","article-title":"Bradykinin-potentiating peptides: beyond captopril","volume":"59","author":"Camargo","year":"2012","journal-title":"Toxicon"},{"issue":"10","key":"10.1016\/j.peptides.2018.01.015_bib0185","doi-asserted-by":"crossref","first-page":"2442","DOI":"10.1111\/j.1742-4658.2008.06389.x","article-title":"A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15","volume":"275","author":"Rioli","year":"2008","journal-title":"FEBS J."},{"issue":"12","key":"10.1016\/j.peptides.2018.01.015_bib0190","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1002\/rcm.1973","article-title":"Fast analysis of low molecular mass compounds present in snake venom: identification of ten new pyroglutamate-containing peptides","volume":"19","author":"Wermelinger","year":"2005","journal-title":"Rapid Commun. Mass Spectrom."},{"issue":"2","key":"10.1016\/j.peptides.2018.01.015_bib0195","doi-asserted-by":"crossref","first-page":"327","DOI":"10.3390\/toxins5020327","article-title":"ESI\u2013MS\/MS identification of a Bradykinin-Potentiating peptide from Amazon Bothrops atrox snake venom using a hybrid qq-oaTOF mass spectrometer","volume":"5","author":"Coutinho-Neto","year":"2013","journal-title":"Toxins"},{"issue":"1\u20133","key":"10.1016\/j.peptides.2018.01.015_bib0200","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0162-3109(96)00018-5","article-title":"Potentiation of the biological efficacy of bradykinin by ACE inhibitors: a shift in the affinity of the B2 receptor?","volume":"33","author":"Hecker","year":"1996","journal-title":"Immunopharmacology"},{"issue":"3","key":"10.1016\/j.peptides.2018.01.015_bib0205","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1161\/01.HYP.33.3.835","article-title":"Enhancement of bradykinin and resensitization of its B2 receptor","volume":"33","author":"Marcic","year":"1999","journal-title":"Hypertension"},{"issue":"5","key":"10.1016\/j.peptides.2018.01.015_bib0210","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1161\/01.RES.81.5.848","article-title":"Potentiation of the actions of bradykinin by angiotensin I-converting enzyme inhibitors. The role of expressed human bradykinin B2 receptors and angiotensin I-converting enzyme in CHO cells","volume":"81","author":"Minshall","year":"1997","journal-title":"Circ. Res."},{"issue":"7","key":"10.1016\/j.peptides.2018.01.015_bib0215","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1016\/j.peptides.2005.03.046","article-title":"Potentiation of bradykinin actions by analogues of the bradykinin potentiating nonapeptide BPP9alpha","volume":"26","author":"Mueller","year":"2005","journal-title":"Peptides"},{"issue":"4","key":"10.1016\/j.peptides.2018.01.015_bib0220","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/S0041-0101(96)00142-0","article-title":"Snakebite by the bushmaster (Lachesis muta) in Brazil: case report and review of the literature","volume":"35","author":"Jorge","year":"1997","journal-title":"Toxicon"}],"container-title":["Peptides"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978118300238?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978118300238?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,10,10]],"date-time":"2019-10-10T01:08:19Z","timestamp":1570669699000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0196978118300238"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4]]},"references-count":44,"alternative-id":["S0196978118300238"],"URL":"https:\/\/doi.org\/10.1016\/j.peptides.2018.01.015","relation":{},"ISSN":["0196-9781"],"issn-type":[{"value":"0196-9781","type":"print"}],"subject":[],"published":{"date-parts":[[2018,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"LmrBPP9: A synthetic bradykinin-potentiating peptide from Lachesis muta rhombeata venom that inhibits the angiotensin-converting enzyme activity in vitro and reduces the blood pressure of hypertensive rats","name":"articletitle","label":"Article Title"},{"value":"Peptides","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.peptides.2018.01.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}