{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,31]],"date-time":"2026-01-31T23:44:23Z","timestamp":1769903063877,"version":"3.49.0"},"reference-count":33,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2016,3,5]],"date-time":"2016-03-05T00:00:00Z","timestamp":1457136000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Science and Technology","award":["MOST 104-2320-B110-002-MY2"],"award-info":[{"award-number":["MOST 104-2320-B110-002-MY2"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Bungarus multicinctus \u03b1-bungarotoxin (\u03b1-Bgt) and Naja atra cardiotoxins (CTXs) share a common structural scaffold, and their tertiary structures adopt three-fingered loop motifs. Four DNA aptamers against \u03b1-Bgt have been reported previously. Given that the binding of aptamers with targeted proteins depends on structural complementarity, in this study, we investigated whether DNA aptamers against \u03b1-Bgt could also recognize CTXs. It was found that N. atra cardiotoxin 3 (CTX3) reduced the electrophoretic mobility of aptamers against \u03b1-Bgt. Analysis of the changes in the fluorescence intensity of carboxyfluorescein-labeled aptamers upon binding toxin molecules revealed that CTX3 and \u03b1-Bgt could bind the tested aptamers. Moreover, the aptamers inhibited the membrane-damaging activity and cytotoxicity of CTX3. In addition to CTX3, other N. atra CTX isotoxins also bound to the aptamer against \u03b1-Bgt. Taken together, our data indicate that aptamers against \u03b1-Bgt show cross-reactivity with CTXs. The findings that aptamers against \u03b1-Bgt also suppress the biological activities of CTX3 highlight the potential utility of aptamers in regard to the broad inhibition of snake venom three-fingered proteins.<\/jats:p>","DOI":"10.3390\/toxins8030066","type":"journal-article","created":{"date-parts":[[2016,3,7]],"date-time":"2016-03-07T10:25:00Z","timestamp":1457346300000},"page":"66","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["DNA Aptamers against Taiwan Banded Krait \u03b1-Bungarotoxin Recognize Taiwan Cobra Cardiotoxins"],"prefix":"10.3390","volume":"8","author":[{"given":"Ying-Jung","family":"Chen","sequence":"first","affiliation":[{"name":"Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chia-Yu","family":"Tsai","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wan-Ping","family":"Hu","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Long-Sen","family":"Chang","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan"},{"name":"Department of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2016,3,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/nrd3141","article-title":"Aptamers as therapeutics","volume":"9","author":"Keefe","year":"2010","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"612","DOI":"10.3390\/s120100612","article-title":"Aptamers and their biological applications","volume":"12","author":"Song","year":"2012","journal-title":"Sensors"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2541","DOI":"10.3390\/toxins6082541","article-title":"Engineering venom\u2019s toxin-neutralizing antibody fragments and its therapeutic potential","volume":"6","author":"Alvarenga","year":"2014","journal-title":"Toxins"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1590\/S1678-91992009000100002","article-title":"Snake antivenoms: Adverse reactions and production technology","volume":"15","author":"Morais","year":"2009","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1067\/mem.2001.113372","article-title":"Efficacy, safety, and use of snake antivenoms in the United States","volume":"37","author":"Dart","year":"2001","journal-title":"Ann. Emerg. Med."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Lauridsen, L.H., Shamaileh, H.A., Edwards, S.L., Taran, E., and Veedu, R.N. (2012). Rapid one-step selection method for generating nucleic acid aptamers: Development of a DNA aptamer against \u03b1-bungarotoxin. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0041702"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Ye, F., Zheng, Y., Wang, X., Tan, X., Zhang, T., Xin, W., Wang, J., Huang, Y., Fan, Q., and Wang, J. (2014). Recognition of Bungarus multicinctus venom by a DNA aptamer against \u03b2-bungarotoxin. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0105404"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1093\/protein\/1.1.37","article-title":"The crystal structure of \u03b1-bungarotoxin at 2.5 \u00c5 resolution: Relation to solution structure and binding to acetylcholine receptor","volume":"1","author":"Love","year":"1986","journal-title":"Protein Eng."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1046\/j.1432-1327.1999.00623.x","article-title":"Snake venom alpha-neurotoxins and other \u201cthree-finger\u201d proteins","volume":"264","author":"Tsetlin","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1002\/jccs.199900048","article-title":"Biochemistry and molecular biology of snake neurotoxin","volume":"46","author":"Yang","year":"1999","journal-title":"J. Chin. Chem. Soc."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1110\/ps.9.4.637","article-title":"Elucidation of the solution structure of cardiotoxin analogue V from the Taiwan cobra (Naja naja atra), identification of structural features important for the lethal action of snake venom cardiotoxins","volume":"9","author":"Jayaraman","year":"2000","journal-title":"Protein Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.toxicon.2010.07.010","article-title":"Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets","volume":"56","author":"Kini","year":"2010","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1080\/15569540701209716","article-title":"Genetic diversity in snake venom three-finger proteins and phospholipase A2 enzymes","volume":"26","author":"Chang","year":"2007","journal-title":"Toxins Rev."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3970","DOI":"10.1093\/nar\/27.20.3970","article-title":"Genetic organization of \u03b1-bungarotoxins from Bungarus multicinctus (Taiwan banded krait): Evidence showing that the production of \u03b1-bungarotoxin isotoxins is not derived from edited mRNAs","volume":"27","author":"Chang","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"i215","DOI":"10.1093\/bioinformatics\/bts210","article-title":"Identification of sequence-structure RNA binding motifs for SELEX-derived aptamers","volume":"28","author":"Hoinka","year":"2012","journal-title":"Bioinformatics"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1093\/nar\/gks979","article-title":"The RNA-binding domain of influenza virus non-structural protein-1 cooperatively binds to virus-specific RNA sequences in a structure-dependent manner","volume":"41","author":"Marc","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1006\/mthe.2001.0495","article-title":"Generation of species cross-reactive aptamers using \u201ctoggle\u201d SELEX","volume":"4","author":"White","year":"2001","journal-title":"Mol. Ther."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e82","DOI":"10.1093\/nar\/gkv534","article-title":"Identifying high-affinity aptamer ligands with defined cross-reactivity using high-throughput guided systematic evolution of ligands by exponential enrichment","volume":"43","author":"Levay","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1016\/j.bios.2008.07.082","article-title":"Detection system based on the conformational change in an aptamer and its application to simple bound\/free separation","volume":"24","author":"Ogasawara","year":"2009","journal-title":"Biosens. Bioelectron."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"10002","DOI":"10.1021\/ac901849k","article-title":"Direct optical detection of aptamer conformational changes induced by target molecules","volume":"81","author":"Neumann","year":"2009","journal-title":"Anal. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1039\/c2nj40501f","article-title":"A simple adenosine fluorescent aptasensor based on the quenching ability of guanine","volume":"36","author":"Fan","year":"2012","journal-title":"New J. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2403","DOI":"10.1021\/bi962594h","article-title":"Crystal structure of cardiotoxin V from Taiwan cobra venom: pH-dependent conformational change and a novel membrane-binding motif identified in the three-finger loops of P-type cardiotoxin","volume":"36","author":"Sun","year":"1997","journal-title":"Biochemistry"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"7414","DOI":"10.1021\/bi050172e","article-title":"Structural difference between group I and group II cobra cardiotoxins: X-ray, NMR, and CD analysis of the effect of cis-proline conformation on three-fingered toxins","volume":"44","author":"Chen","year":"2005","journal-title":"Biochemistry"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/978-1-4613-0361-9_7","article-title":"A case study of cardiotoxin III from the Taiwan cobra (Naja naja atra). Solution structure and other physical properties","volume":"391","author":"Kumar","year":"1996","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"205102","DOI":"10.1088\/0957-4484\/19\/20\/205102","article-title":"\u03b1-Bungarotoxin binding to target cell in a developing visual system by carboxylated nanodiamond","volume":"19","author":"Liu","year":"2008","journal-title":"Nanotechnology"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"8046","DOI":"10.1021\/bi00399a004","article-title":"Role of tyrosine and tryptophan residues in the structure-activity relationships of a cardiotoxin from Naja nigricollis venom","volume":"26","author":"Gatineau","year":"1987","journal-title":"Biochemisrty"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"6480","DOI":"10.1021\/bi00479a021","article-title":"Delineation of the functional site of a snake venom cardiotoxin: Preparation, structure, and function of monoacetylated derivatives","volume":"29","author":"Gatineau","year":"1990","journal-title":"Biochemistry"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1006\/taap.1996.0162","article-title":"Chemical modification of methionines in a cobra venom cytotoxin differentiates between lytic and binding domains","volume":"139","author":"Hinman","year":"1996","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/S0041-0101(96)00188-2","article-title":"Activities of cobra venom cytotoxins toward heart and leukemic T-cells depend on localized amino acid differences","volume":"35","author":"Hinman","year":"1997","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1042\/bj20020437","article-title":"Cytotoxic potency of cardiotoxin from Naja sputatrix: Development of a new cytolytic assay","volume":"366","author":"Ma","year":"2002","journal-title":"Biochem. J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4411","DOI":"10.1016\/j.bios.2011.04.053","article-title":"Selection of thrombin-binding aptamers by using computational approach for aptasensor application","volume":"26","author":"Bini","year":"2011","journal-title":"Biosens. Bioelectron."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"11777","DOI":"10.1093\/nar\/gks899","article-title":"Selection is more intelligent than design: Improving the affinity of a bivalent ligand through directed evolution","volume":"40","author":"Ahmad","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1023\/A:1014520126856","article-title":"Separation and structure-function studies of Taiwan cobra cardiotoxins","volume":"21","author":"Lin","year":"2002","journal-title":"J. Protein Chem."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/8\/3\/66\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T19:20:14Z","timestamp":1760210414000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/8\/3\/66"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,3,5]]},"references-count":33,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2016,3]]}},"alternative-id":["toxins8030066"],"URL":"https:\/\/doi.org\/10.3390\/toxins8030066","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,3,5]]}}}