dc.contributor.author | Andre, Sabine | |
dc.contributor.author | Wang, Guan-Nan | |
dc.contributor.author | Gabius, Hans-Joachim | |
dc.contributor.author | Murphy, Paul V. | |
dc.date.accessioned | 2015-12-10T14:33:04Z | |
dc.date.issued | 2014-05-07 | |
dc.identifier.citation | Andre, S,Wang, GN,Gabius, HJ,Murphy, PV (2014) 'Combining glycocluster synthesis with protein engineering: an approach to probe into the significance of linker length in a tandem-repeat-type lectin (galectin-4)'. Carbohydrate Research, 389 :25-38. | en_IE |
dc.identifier.issn | 1873-426X | |
dc.identifier.uri | http://hdl.handle.net/10379/5382 | |
dc.description.abstract | Complementarity in lectin-glycan interactions in situ is assumed to involve spatial features in both the lectin and the glycan, giving a functional meaning to structural aspects of the lectin beyond its carbohydrate-binding site. In combining protein engineering with glycocluster synthesis, it is shown that the natural linker length of a tandem-repeat-type human lectin (galectin-4) determines binding properties in two binding assays (using surface-presented glycoprotein and cell surface assays). The types of glycocluster tested included bivalent lactosides based on tertiary amides of terephthalic, isophthalic, 2,6-naphthalic and oxalic acids as well as bivalent H(type 2) trisaccharides grafted on secondary/tertiary terephthalamides and two triazole-linker-containing cores. The presented data reveal a marked change in susceptibility to the test compounds when turning the tandem-repeat-type to a proto-type-like display. The testing of glycoclusters is suggested as a general strategy to help to delineate the significance of distinct structural features of lectins beyond their contact sites to the glycan. (C) 2014 Elsevier Ltd. All rights reserved. | en_IE |
dc.description.sponsorship | Science Foundation Ireland (08/SRC/B1393), the EC research/ITN programs GlycoHIT (contract no. 260600), COST (CM1102) and GLYCOPHARM (contract no. 217297) and the Verein zur Förderung des biologisch-technologischen Fortschritts in der Medizin e.V | en_IE |
dc.format | application/pdf | en_IE |
dc.language.iso | en | en_IE |
dc.publisher | Elsevier | en_IE |
dc.relation.ispartof | Carbohydrate Research | en |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Ireland | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/ie/ | |
dc.subject | Agglutinin | en_IE |
dc.subject | Glycoprotein | en_IE |
dc.subject | Lectin | en_IE |
dc.subject | Modelling | en_IE |
dc.subject | Terephthalamides | en_IE |
dc.subject | Triazoles | en_IE |
dc.subject | Enterocyte-like cells | en_IE |
dc.subject | Pancreatic-carcinoma model | en_IE |
dc.subject | Human neuroblastoma-cells | en_IE |
dc.subject | Sugar code | en_IE |
dc.subject | Tetravalent glycoclusters | en_IE |
dc.subject | Molecular switches | en_IE |
dc.subject | Relevant lectins | en_IE |
dc.subject | Terminal alkynes | en_IE |
dc.subject | Surface binding | en_IE |
dc.subject | Down-regulation | en_IE |
dc.title | Combining glycocluster synthesis with protein engineering: an approach to probe into the significance of linker length in a tandem-repeat-type lectin (galectin-4) | en_IE |
dc.type | Article | en_IE |
dc.date.updated | 2015-11-30T12:11:06Z | |
dc.identifier.doi | 10.1016/j.carres.2013.12.024 | |
dc.local.publishedsource | http://dx.doi.org/10.1016/j.carres.2013.12.024 | en_IE |
dc.description.peer-reviewed | peer-reviewed | |
dc.contributor.funder | |~| | |
dc.description.embargo | 2016-05-07 | |
dc.internal.rssid | 6391373 | |
dc.local.contact | Paul Murphy, School Of Chemistry, Room 236, Arts/Science Building, Nui Galway. 2465 Email: paul.v.murphy@nuigalway.ie | |
dc.local.copyrightchecked | No | |
dc.local.version | SUBMITTED | |
nui.item.downloads | 474 | |