Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules.

Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Research Abstract Details 

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Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Abstract Text:

Karin Enander,Gunnar T Dolphin,Lars Baltzer,

Polypeptides designed to fold into helix-loop-helix motifs and to dimerize to form four-helix bundles were functionalized by the introduction of a sulfonamide derivative known to bind human carbonic anhydrase II (HCAII) and one or both of the dansyl- and methoxycoumarin fluorescent probes. The 42-residue sequence DC that carries all three substituents in solvent-exposed positions was found to bind HCAII with a dissociation constant of 5 nM in aqueous solution at pH 7. At 2 muM concentration, DC was mainly dimeric in aqueous solution but bound HCAII as a monomer. Upon addition of a large excess of a helix-loop-helix motif without a high-affinity ligand, KE2-Q, a ternary complex was formed between HCAII, DC, and KE2-Q. Hydrophobic interactions between DC and HCAII and coordination of the sulfonamide group to the zinc ion of HCAII contributed cooperatively to binding in a demonstration of the usefulness of folded polypeptide-small organic molecule chimera as novel protein receptors. The DC homodimer was found to be a very sensitive biosensor component due to intermolecular quenching of its fluorescence that was inhibited upon binding to HCAII.

Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Publishing Authors By Initials

K Enander,GT Dolphin,L Baltzer,

For similar investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research abstracts see: investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research

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Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Chemical Society

VOLUME: 126

Page Numbers: 4464-5

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 14

MONTH: Apr

YEAR: 2004

Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Fluorescence

MESH TERMS: metabolism

Chemical & Substance for Abstract: Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules. Information

Substance Name: Carbonic Anhydrase II

Registry Number: EC 4.2.1.-

Grant and Affiliation Information for Designed, functionalized helix-loop-helix motifs that bind human carbonic anhydrase II: a new class of synthetic receptor molecules.

AFFILIATION: Department of Chemistry-IFM, Linköping University, 581 83 Linköping, Sweden.

Country: United States

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MEDLINETA: J Am Chem Soc

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