A trivalent system from vancomycin-D-Ala-D-Ala with higher affinity than avidin-biotin

Science

Volumn 280, Issue 5364, 1998, Pages 708-711

  Rao, Jianghong ^a   Lahiri, Joydeep ^a   Isaacs, Lyle ^a   Weis, Robert M ^b   Whitesides, George M ^a  

^a HARVARD UNIVERSITY   (United States)

^b UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AVIDIN; BIOTIN; VANCOMYCIN DERIVATIVE;

ARTICLE; BINDING AFFINITY; CALORIMETRY; DISSOCIATION CONSTANT; DRUG PROTEIN BINDING; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ALANINE; AVIDIN; BIOTIN; CALORIMETRY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIPEPTIDES; KINETICS; LIGANDS; THERMODYNAMICS; VANCOMYCIN;

EID: 0032076568     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5364.708     Document Type: Article

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29. 3 have larger sizes and more conformational freedom than V and L. The next two steps would be less entropically unfavorable than the first binding event, because they take place intramolecularly.
30. Supported by NIH grants GM 30367 (G.M.W.), GM 51559 (G.M.W.), and GM 53210 (R.M.W.). J.R. thanks Eli Lilly (1996-97) and Hoffmann-LaRoche (1997-98) for doctoral fellowships. L.I. thanks NIH for a postdoctoral fellowship.