Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/61106
DC Field | Value | Language |
---|---|---|
dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Liu, J | - |
dc.creator | Liu, M | - |
dc.creator | Zheng, B | - |
dc.creator | Yao, Z | - |
dc.creator | Xia, J | - |
dc.date.accessioned | 2016-12-19T08:54:44Z | - |
dc.date.available | 2016-12-19T08:54:44Z | - |
dc.identifier.uri | http://hdl.handle.net/10397/61106 | - |
dc.language.iso | en | en_US |
dc.publisher | Public Library of Science | en_US |
dc.rights | © 2016 Liu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | en_US |
dc.rights | The following publication: Liu J, Liu M, Zheng B, Yao Z, Xia J (2016) Affinity Enhancement by Ligand Clustering Effect Inspired by Peptide Dendrimers−Shank PDZ Proteins Interactions. PLoS ONE 11(2): e0149580 is available at https://doi.org/10.1371/journal.pone.0149580 | en_US |
dc.title | Affinity enhancement by ligand clustering effect inspired by peptide dendrimers-shank PDZ proteins interactions | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.volume | 11 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.doi | 10.1371/journal.pone.0149580 | en_US |
dcterms.abstract | High-affinity binders are desirable tools to probe the function that specific protein-protein interactions play in cell. In the process of seeking a general strategy to design high-affinity binders, we found a clue from the βPIX (p21-activated kinase interacting exchange factor) -Shank PDZ interaction in synaptic assembly: three PDZ-binding sites are clustered by a parallel coiled-coil trimer but bind to Shank PDZ protein with 1:1 stoichiometry (1 trimer/1 PDZ). Inspired by this architecture, we proposed that peptide dendrimer, mimicking the ligand clustering in βPIX, will also show enhanced binding affinity, yet with 1:1 stoichiometry. This postulation has been proven here, as we synthesized a set of monomeric, dimeric and trimeric peptides and measured their binding affinity and stoichiometry with Shank PDZ domains by isothermal titration calorimetry, native mass spectrometry and surface plasmon resonance. This affinity enhancement, best explained by proximity effect, will be useful to guide the design of high-affinity blockers for protein-protein interactions. | - |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | PLoS one, 2016, v. 11, no. 2, e0149580 | - |
dcterms.isPartOf | PLoS one | - |
dcterms.issued | 2016 | - |
dc.identifier.isi | WOS:000371274400025 | - |
dc.identifier.scopus | 2-s2.0-84960414248 | - |
dc.identifier.pmid | 26918521 | - |
dc.identifier.eissn | 1932-6203 | en_US |
dc.identifier.rosgroupid | 2015003509 | - |
dc.description.ros | 2015-2016 > Academic research: refereed > Publication in refereed journal | en_US |
dc.description.validate | 201810_a bcma | en_US |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
Files in This Item:
File | Description | Size | Format | |
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Liu_Affinity_enhancement_ligand.PDF | 2.25 MB | Adobe PDF | View/Open |
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