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Titolo:
Biotin reagents for antibody pretargeting. 5. Additional studies of biotinconjugate design to provide biotinidase stability
Autore:
Wilbur, DS; Hamlin, DK; Chyan, MK; Kegley, BB; Pathare, PM;
Indirizzi:
Univ Washington, Dept Radiat Oncol, Seattle, WA 98103 USA Univ WashingtonSeattle WA USA 98103 Radiat Oncol, Seattle, WA 98103 USA
Titolo Testata:
BIOCONJUGATE CHEMISTRY
fascicolo: 4, volume: 12, anno: 2001,
pagine: 616 - 623
SICI:
1043-1802(200107/08)12:4<616:BRFAP5>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-SERUM BIOTINIDASE; TUMOR-LOCALIZATION; AVIDIN; STREPTAVIDIN; DERIVATIVES; BINDING; RADIOIMMUNOTHERAPY; RADIOASSAY; RESISTANT; TISSUES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Wilbur, DS Univ Washington, Dept Radiat Oncol, 2121 N 35th St, Seattle, WA98103 USA Univ Washington 2121 N 35th St Seattle WA USA 98103 A 98103 USA
Citazione:
D.S. Wilbur et al., "Biotin reagents for antibody pretargeting. 5. Additional studies of biotinconjugate design to provide biotinidase stability", BIOCONJ CHE, 12(4), 2001, pp. 616-623

Abstract

An investigation was conducted in which the stabilities of four structurally different biotin derivatives were assessed with regard to biotinamide bond hydrolysis by the enzyme biotinidase. The biotin derivatives studied contained an extra methylene in the valeric acid chain of biotin (i.e., homobiotin), or contained conjugated amino acids having hydroxymethylene, carboxylate, or acetate functionalities on a methylene alpha to the biotinamide bond. The biotinidase hydrolysis assay was conducted on biotin derivatives that were radioiodinated at high specific activity, and then subjected to diluted human serum at 37 degreesC for 2 h. After incubation, assessment of biotinamide bond hydrolysis by biotinidase was readily achieved by measuring the percentage of radioactivity that did not bind with avidin. As controls,an unsubstituted biotin derivative which is rapidly cleaved by biotinidaseand an N-methyl-substituted biotin derivative which is stable to biotinidase cleavage were included in the study. The results indicate that increasing the distance from the biotin ring structure to the biotinamide bond by one methylene only decreases the rate of biotinidase cleavage, but does not block it. The data obtained also indicate that placing a hydroxymethylene, carboxylate, or acetate alpha to the biotinamide bond is effective in blocking the biotinamide hydrolysis reaction. These data, in combination with data previously obtained, which indicate that biotin derivatives containing hydroxymethylene or carboxylate moieties retain the slow dissociation rate ofbiotin from avidin and streptavidin [Wilbur, D. S., et al. (2000) Bioconjugate Chem. 11, 569-583], strongly support incorporation of these structuralfeatures into biotin derivatives being used for in vivo targeting applications.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 18:00:37