Facile supermolecular aptamer inhibitors of L-selectin.

Multivalent interactions occur frequently in nature, where they mediate high-affinity interactions between cells, proteins, or molecules. Here, we report on a method to generate multivalent aptamers (Multi-Aptamers) that target L-selectin function using rolling circle amplification (RCA). We find th...

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Main Authors: Elizabeth K Chang, Mark A Eckert, M Monsur Ali, Hamidreza Riazifar, Egest J Pone, Linan Liu, Weian Zhao
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4380364?pdf=render
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spelling doaj-b81f35e73872422abe79aef1ec074a722020-11-24T21:30:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01103e012303410.1371/journal.pone.0123034Facile supermolecular aptamer inhibitors of L-selectin.Elizabeth K ChangMark A EckertM Monsur AliHamidreza RiazifarEgest J PoneLinan LiuWeian ZhaoMultivalent interactions occur frequently in nature, where they mediate high-affinity interactions between cells, proteins, or molecules. Here, we report on a method to generate multivalent aptamers (Multi-Aptamers) that target L-selectin function using rolling circle amplification (RCA). We find that the L-selectin Multi-Aptamers have increased affinity compared to the monovalent aptamer, are specific to L-selectin, and are capable of inhibiting interactions with endogenous ligands. In addition, the Multi-Aptamers efficiently inhibit L-selectin mediated dynamic adhesion in vitro and homing to secondary lymphoid tissues in vivo. Importantly, our method of generating multivalent materials using RCA avoids many of the challenges associated with current multivalent materials in that the Multi-Aptamers are high affinity, easily produced and modified, and biocompatible. We anticipate that the Multi-Aptamers can serve as a platform technology to modulate diverse cellular processes.http://europepmc.org/articles/PMC4380364?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Elizabeth K Chang
Mark A Eckert
M Monsur Ali
Hamidreza Riazifar
Egest J Pone
Linan Liu
Weian Zhao
spellingShingle Elizabeth K Chang
Mark A Eckert
M Monsur Ali
Hamidreza Riazifar
Egest J Pone
Linan Liu
Weian Zhao
Facile supermolecular aptamer inhibitors of L-selectin.
PLoS ONE
author_facet Elizabeth K Chang
Mark A Eckert
M Monsur Ali
Hamidreza Riazifar
Egest J Pone
Linan Liu
Weian Zhao
author_sort Elizabeth K Chang
title Facile supermolecular aptamer inhibitors of L-selectin.
title_short Facile supermolecular aptamer inhibitors of L-selectin.
title_full Facile supermolecular aptamer inhibitors of L-selectin.
title_fullStr Facile supermolecular aptamer inhibitors of L-selectin.
title_full_unstemmed Facile supermolecular aptamer inhibitors of L-selectin.
title_sort facile supermolecular aptamer inhibitors of l-selectin.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2015-01-01
description Multivalent interactions occur frequently in nature, where they mediate high-affinity interactions between cells, proteins, or molecules. Here, we report on a method to generate multivalent aptamers (Multi-Aptamers) that target L-selectin function using rolling circle amplification (RCA). We find that the L-selectin Multi-Aptamers have increased affinity compared to the monovalent aptamer, are specific to L-selectin, and are capable of inhibiting interactions with endogenous ligands. In addition, the Multi-Aptamers efficiently inhibit L-selectin mediated dynamic adhesion in vitro and homing to secondary lymphoid tissues in vivo. Importantly, our method of generating multivalent materials using RCA avoids many of the challenges associated with current multivalent materials in that the Multi-Aptamers are high affinity, easily produced and modified, and biocompatible. We anticipate that the Multi-Aptamers can serve as a platform technology to modulate diverse cellular processes.
url http://europepmc.org/articles/PMC4380364?pdf=render
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