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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b00735
|2 doi
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|a pubmed24n0947.xml
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|a (DE-627)NLM284299154
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|a (NLM)29783836
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|a DE-627
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|e rakwb
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|a eng
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|a Senapati, Subhadip
|e verfasserin
|4 aut
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|a A Y-Shaped Three-Arm Structure for Probing Bivalent Interactions between Protein Receptor-Ligand Using AFM and SPR
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 29.03.2019
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|a Date Revised 29.03.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The goal of this research was to develop linkage chemistry for the study of bivalent interactions between a receptor and its ligand using atomic force microscopy (AFM) and surface plasmon resonance (SPR). We conceived a three-arm structure composed of flexible chains connected to a large rigid core with orthogonal functional groups at their ends for formation and attachment (or immobilization) of bivalent ligands. To demonstrate the principle, we chose the well-known biotin-streptavidin interaction as a model system. On the basis of a crystal structure of the biotin-streptavidin complex, we designed and synthesized a bisbiotin ligand to have a Y shape with two biotin motifs on its arms for binding and a functional group on its stem for immobilization or attachment, referred to as y-bisbiotin. First, we found that the y-bisbiotin ligand stabilized the streptavidin more than its monobiotin counterpart did in solution, which indicates that the bivalent interaction was synergistic. The y-bisbiotin was attached to AFM tips through a click reaction for the force measurement experiments, which showed that unbinding the bisbiotin from streptavidin needed twice the force of unbinding a monobiotin. For the SPR study, we added a ω-thiolated alkyl chain to y-bisbiotin for its incorporation into a monolayer. The SPR data indicated that the streptavidin dissociated from a mixed monolayer bearing y-bisbiotin much slower than from the one bearing monobiotin. This work demonstrates unique chemistry for the study of bivalent interactions using AFM and SPR
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Ligands
|2 NLM
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|a Proteins
|2 NLM
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|a Biotin
|2 NLM
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|a 6SO6U10H04
|2 NLM
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|a Streptavidin
|2 NLM
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|a 9013-20-1
|2 NLM
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| 700 |
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|a Biswas, Sudipta
|e verfasserin
|4 aut
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|a Manna, Saikat
|e verfasserin
|4 aut
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| 700 |
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|a Ros, Robert
|e verfasserin
|4 aut
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| 700 |
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|a Lindsay, Stuart
|e verfasserin
|4 aut
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| 700 |
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|a Zhang, Peiming
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 34(2018), 23 vom: 12. Juni, Seite 6930-6940
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:34
|g year:2018
|g number:23
|g day:12
|g month:06
|g pages:6930-6940
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|u http://dx.doi.org/10.1021/acs.langmuir.8b00735
|3 Volltext
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