The Tryptophan Fluorescence of Tetracarbidium conophorum Agglutinin II and a Solution-Based Assay for the Binding of a Biantennary Glycopeptide |
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| Authors: | Martha P. Brown Dimitri Toptygin K. B. Lee Theresa Animashaun R. C. Hughes Y. C. Lee Ludwig Brand |
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| Affiliation: | (1) Department of Biology, The Johns Hopkins University, Mudd Hall, Baltimore, Maryland, 21218;(2) National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom;(3) Present address: School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin, 53706 |
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| Abstract: | The plant lectin Tetracarbidium conophorum agglutinin II binds to glycoproteins and glycopeptides in a structurally specific manner [Animashaun et al., (1994) Glycoconjugate J.11, 299–303]. We have characterized the steady-state and time-resolved fluorescence of the tryptophan residues of this lectin. The fluorescence ( ex = 295 nm, em = 350 nm) decay is complex and can be described by four decay times with the following values:  1 = 7.4nsec,  1 = 0.22; 2 = 2.9 nsec, 2 = 0.25; 3 = l.0 nsec, 3 = 0.34; 4 = 0.2 nsec, 4 = 0.18. The addition of a biantennary glycopeptide  to the lectin results in a quench and an 8 nm blue shift of the emission spectrum. The effect is saturable, and is described by an association constant of 1.8×105 M–1. The tryptophan fluorescence of Tetracarbidium conophorum agglutinin II may therefore be utilized to characterize thermodynamically the binding interactions between this lectin and complex glycoprotein. |
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| Keywords: | Lectin tryptophan fluorescence lifetime glycopeptide |
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