{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:25:03Z","timestamp":1791354303932,"version":"4.3.1"},"reference-count":41,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2009,4,21]],"date-time":"2009-04-21T00:00:00Z","timestamp":1240272000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2009,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Mucins form a group of heavily <jats:italic>O<\/jats:italic>\u2010glycosylated biologically important glycoproteins that are involved in a variety of biological functions, including modulating immune response, inflammation, and adhesion. Mucins are also involved in cancer and metastasis and often express diagnostic cancer antigens. Recently, a modified porcine submaxillary mucin (Tn\u2010PSM) containing GalNAc\u03b11\u2010<jats:italic>O<\/jats:italic>\u2010Ser\/Thr residues was shown to bind to soybean agglutinin (SBA) with \u223c10<jats:sup>6<\/jats:sup>\u2010fold enhanced affinity relative to GalNAc\u03b11\u2010<jats:italic>O<\/jats:italic>\u2010Ser, the pancarcinoma carbohydrate antigen. In this study, dynamic force spectroscopy is used to investigate molecular pairs of SBA and Tn\u2010PSM. A number of force jumps that demonstrate unbinding or rebinding events were observed up to a distance equal to 2.0 \u03bcm, consistent with the length of the mucin chain. The unbinding force increased from 103 to 402 pN with increasing force loading rate. The position of the activation barrier in the energy landscape of the interaction was 0.1 nm. The lifetime of the SBA\u2013TnPSM complex in the absence of applied force was determined to be in the range 1.3\u20131.9 s. Kinetic parameters describing the rate of dissociation of other sugar lectin interactions are in the range 3.3 \u00d7 10<jats:sup>\u22123<\/jats:sup>\u20132.5 \u00d7 10<jats:sup>\u22123<\/jats:sup> s. The long lifetime of the SBA\u2010TnPSM complex is compatible with a binding model in which lectin molecules \u201cbind and jump\u201d from \u03b1\u2010GalNAc residue to \u03b1\u2010GalNAc residue along the polypeptide chain of Tn\u2010PSM before dissociating. These findings have important implications for the molecular recognition properties of mucins. \u00a9 2009 Wiley Periodicals, Inc. Biopolymers 91: 719\u2013728, 2009.<\/jats:p><jats:p>This article was originally published online as an accepted preprint. The \u201cPublished Online\u201d date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com<\/jats:p>","DOI":"10.1002\/bip.21213","type":"journal-article","created":{"date-parts":[[2009,4,21]],"date-time":"2009-04-21T18:22:51Z","timestamp":1240338171000},"page":"719-728","source":"Crossref","is-referenced-by-count":28,"title":["Single\u2010molecule pair studies of the interactions of the \u03b1\u2010GalNAc (Tn\u2010antigen) form of porcine submaxillary mucin with soybean agglutinin"],"prefix":"10.1002","volume":"91","author":[{"given":"Marit","family":"Sletmoen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tarun K.","family":"Dam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas A.","family":"Gerken","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bj\u00f8rn T.","family":"Stokke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Curtis Fred","family":"Brewer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,4,21]]},"reference":[{"key":"e_1_2_5_2_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1025815113599"},{"key":"e_1_2_5_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0304-4165(02)00409-9"},{"key":"e_1_2_5_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrc1251"},{"key":"e_1_2_5_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmc.2005.04.085"},{"key":"e_1_2_5_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/10.5.439"},{"key":"e_1_2_5_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.012540899"},{"key":"e_1_2_5_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tcb.2006.07.006"},{"key":"e_1_2_5_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrd1751"},{"key":"e_1_2_5_10_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M606862200"},{"key":"e_1_2_5_11_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi036306a"},{"key":"e_1_2_5_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.52.33204"},{"key":"e_1_2_5_13_2","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1016\/S0021-9258(18)93649-5","volume":"243","author":"Carlson D. 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