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Poly(N-isopropylacrylamide-co-tris-nitrilotriacetic acid acrylamide) for a Combined Study of Molecular Recognition and Spatial Constraints in Protein Binding and Interactions

Liu, Juan and Spulber, Mariana and Wu, Dalin and Talom, Renee M. and Palivan, Cornelia G. and Meier, Wolfgang. (2014) Poly(N-isopropylacrylamide-co-tris-nitrilotriacetic acid acrylamide) for a Combined Study of Molecular Recognition and Spatial Constraints in Protein Binding and Interactions. Journal of the American Chemical Society, 136 (36). pp. 12607-12614.

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Official URL: http://edoc.unibas.ch/dok/A6329073

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Abstract

Many biological processes require precise regulation and synergy of proteins, and consequently involve molecular recognition and spatial constraints between biomolecules. Here, a library of poly(N-isopropylacrylamide-co-tris-nitrilotriacetic acid acrylamide) (PNTs) has been synthesized and complexed with Cu2+ in order to serve as models for investigation of the combined effects of molecular recognition and spatial constraints in biomolecular interactions. The average distance between Cu2+–trisNTA binding sites in PNTs polymers was varied from 4.3 to 31.5 nm by adjusting their trisNTA contents. His tag (His6), His-tagged enhanced yellow fluorescent protein (His6-eYFP), and His6-tagged collagenase G (His6-ColG), with sizes ranging from 1 to 11 nm, were used as models to assess whether the binding ability is influenced by a cooperative topology based on molecular recognition interactions with Cu2+–trisNTA binding sites, and spatial constraints created by decreasing average distance between trisNTAs. His-tagged molecules bound to all PNTs polymers due to their molecular recognition interaction involving histidines and Cu2+–trisNTA pockets, but with a binding ability that was highly modulated by the average distance between the trisNTA binding sites. Small molecular mass molecules (His6) exhibit a high binding ability to all PNTs polymers, whereas his-tagged proteins bind to PNTs efficiently only when the average distance between trisNTA binding sites is larger than the protein dimensions.
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Makromolekulare Chemie (Meier)
UniBasel Contributors:Meier, Wolfgang P. and Palivan, Cornelia G
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
ISSN:0002-7863
e-ISSN:1520-5126
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:10 Apr 2017 07:11
Deposited On:06 Feb 2015 09:59

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