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Biomedical subjects

A D Broom

Publications and source records attributed to A D Broom.

At least 19 recordsLinked to original sources

Synthesis of oligonucleotides containing 2'-deoxy-6-thioguanosine at a predetermined site.

A new approach has been devised for the synthesis of oligonucleotides containing 2'-deoxy-6-thioguanosine [d(s6G)]. The synthesis of oligonucleotides containing d(s6G) requires special protection and deprotection strategies to prevent the thione functionality from undergoing oxidation and hydrolysis. Previous attempted syntheses have neglected to address this problem. By using the cyanoethyl protecting group for the thione and phenoxyacetyl for the exocyclic amino group, it was possible to deprotect oligonucleotides with a mixture of sodium hydroxide and sodium hydrogen sulfide without any significant conversion of d(s6G) to deoxyguanosine. Application of this strategy will allow investigation of the structural as well as biological activity of d(s6G)-containing oligonucleotides.

Chromatography, High Pressure Liquid

Cytotoxicity, uptake, polyglutamate formation, and antileukemic effects of 8-deaza analogues of methotrexate and aminopterin in mice.

In contrast to methotrexate (MTX) and aminopterin (AMT), the 8-deaza analogues of these antifolates are not substrates for rabbit liver aldehyde oxidase. Since they are not converted to 7-hydroxy derivatives, they have been investigated with regard to their cytotoxicity for CCRF-CEM cells, transport into these cells, and conversion to polyglutamate forms. For this purpose 3H-labeled analogues were synthesized. The drug concentrations of the analogues required to inhibit cell growth by 50% are significantly lower than for the parent compounds particularly for a short exposure of cells to the drug. Vmax and Km for unidirectional influx do not differ greatly among the four drugs, but amounts of uptake over 1 h are markedly different and increase in the order MTX less than 8-deazaMTX less than AMT less than 8-deazaAMT. During 1 h of uptake a much greater proportion of the 8-deaza analogues is converted to polyglutamate forms than in the case of parent drugs. Only 52% of MTX is converted to polyglutamates, whereas in the case of the other three compounds the conversion is greater than or equal to 90%. However, MTX is relatively efficient in adding two glutamate residues, whereas the other drugs predominantly accumulate as forms with only one additional glutamate (+Glu1). During 1 h of efflux the drugs without additional glutamates decrease to low concentrations and there is also a major loss of +Glu1 form, but there is also an increase in longer chain forms, especially in the case of MTX. The net result is a still greater disparity in total intracellular levels of the four drugs after the period of efflux. MTX has much lower toxicity in mice in vivo than the other three compounds, 8-deazaAMT being the most toxic. At the maximum tolerated dose MTX produced a considerably greater increase in life span for mice bearing P388 than any of the other drugs, and a somewhat greater increase for mice bearing L1210. Thus the 8-deaza analogues do not offer a therapeutic advantage over MTX against leukemias in the mouse, primarily due to their much greater toxicity.

Aminopterin

A pyrimidine-based "flexible" bisubstrate analogue inhibitor of human thymidylate synthase.

The synthesis and characterization of two "flexible" bisubstrate analogues of the intermediate in the thymidylate synthase reaction are reported. Steric constraints are minimized and diasteromeric mixtures avoided by using a pyrimidine-based analogue as the folate portion of the inhibitor while retaining all known important binding sites. A preliminary assessment of certain conformational parameters by NMR is presented. The compounds are shown to be potent competitive inhibitors with respect to dUMP or 5,10-CH2-H4PteGlu but gave mixed kinetics with respect to 5,10-CH2-H4PteGlu5 for human thymidylate synthase.

Binding Sites

Folate analogues as inhibitors of thymidylate synthase.

Recent demonstrations that deazafolate analogues may act as potent inhibitors of thymidylate synthase (TS) provided a firm rationale for the synthesis of N10-propargyl derivatives of 8-deazafolate and 8-deazaaminopterin (4). A complete assignment of the 1H NMR spectra of these compounds was made possible through application of 2D (COSY) techniques at 200 MHz. Data describing the inhibition of TS derived from human leukemia (K562) cells are presented. IC50 values of 2.25 and 1.26 microM were determined for 8-deaza-10-propargylfolate (3) and 8-deaza-10-propargylaminopterin, respectively. Comparison of the data for various folate analogues reveals a striking dependence of TS inhibitory potency upon the number of nitrogens in the folate pyrazine ring.

Aminopterin

Design and synthesis of multisubstrate analog inhibitors of one-carbon transfer reactions.

The design and synthesis of multisubstrate analog enzyme inhibitors offer new opportunities in the creation of potent, highly specific drug molecules. Selected examples of inhibitors of 1-carbon transfer serve to illustrate the potential of this approach. Inhibitors of indole-N-methyltransferase, L-aspartyl transcarbamoylase, and thymidylate synthase are illustrative of many compounds that have demonstrated considerable specificity and potency. Several of these inhibitors and the rationale for their syntheses are described.

Antineoplastic Agents

Poly(2-fluoroadenylic acid). The role of basicity in the stabilization of complementary helices.

The polymerization of 2-fluoroadenosine 5'-diphosphate by polynucleotide phosphorylase to give high molecular weight poly(2-fluoroadenylic acid), poly(fl2A), is described. Both the single-stranded and double-stranded (acid) forms of poly(fl2A) exhibit strikingly similar ultraviolet and circular dichroism spectra to those of poly(A), and the enzymatic polymerization rates and thermal hyperchromicities of the two polymers are also very similar. However, the pKa of poly(fl2A) for protonation at N-1 is 2.9 compared to 5.9 for poly(A) under similar conditions. Poly(fl2A) forms a triple-stranded helix with poly(U) which has ultraviolet and cd spectra very reminiscent of poly(A) . 2 poly(U), but no conditions could be found which permitted the formation of a double helix. In the Escherichia coli ribosome system poly(fl2A) codes for the synthesis of polylysine, as does poly(A), although the rate and extent of incorporation were less in the former case. The role of basicity of adenine N-1 in these interactions is discussed.

Drug Stability

Raman spectral studies of poly(1-methylinosinic acid).

The synthesis and characterization of poly(1-methylinosinic acid) are described. Laser Raman spectra of poly (mII) were obtained as a function of temperature in D2O solution. Thermal melting profiles derived from the intensity variations of the 712, 795, 814, 986, 1333, 1509, 1550 and 1680 cm-1 bands indicate a cooperative melting temperature of 9 +/- 1 degree C. The low temperature form of poly(mII) exhibits a carbonyl frequency at 1710 cm-I which is decreased to 1680 cm-I upon melting. The Raman hypochromism in the bands reported are equal to or much larger than any reported for other nucleic acids. The data are consistent with the low temperature form of poly(mII) being an ordered single stranded unit with a high degree of basestacking. The melting profiles obtained from the uv and cd spectra are consistent with and support the Raman data. This single stranded RNA exhibits an uncharacteristic behavior in that it melts cooperatively.

Circular Dichroism

Polyribonucleotides containing thiopurines. Synthesis and properties of poly(1-methyl-6-thioguanylic acid).

The synthesis of 1-methyl-6-thioguanosine 5'-diphosphate and its conversion to poly(1-methyl-6-thioguanylic acid) by means of polynucleotide phosphorylase are described. The polymer exhibited cooperative behavior (Tm = 294 K in the absence of added NaCl) characteristic of a highly stacked single-stranded helical array. In a high salt environment (0.5 M NaCl) the melting was much less cooperative and gave a higher Tm (313 K); this is suggestive of interstrand aggregation involving hydrogen bonding. The polynucleotide exhibited a remarkably high pKa (6.2) compared to that of the mononucleotide (2.6), and formed a very stable acid structure (Tm = 356 K in 50% ethylene glycol). Comparisons with poly(1-methyl-6-thioinosinic acid) and poly(6-thioguanylic acid) establish that both the 2-amino group and the 1-methyl group are required for the formation of the stable acid structure.

Alkaline Phosphatase

Polyribonucleotides containing thiopurines: synthesis and properties of poly (6-thioguanylic acid).

The synthesis of poly(2-amino-6-chloropurinylic acid) [poly(n2cl6Pu)] by the polynucleotide phosphorylase catalyzed polymerization of 2-amino-6-chloro-9-(beta-D-ribofuranosyl)purine 5'-diphosphate and its chemical conversion to poly(6-thioguanylic acid) [poly(s6G)] is described. Poly(s6G) was found to form a relatively unstable complex with poly(C), the properties of which were incompatible with those previously reported for the same complex prepared by another method [Darlix, J.L., Fromageot, P., and Reich, E. (1973), Biochemistry 12, 914]. It was found that poly(s6G) could be thermally converted to a copolymer of which with poly(C) was strikingly similar to that reported earlier for poly(s6G)-poly(C).

Micrococcus

Combined enzymatic and chemical approaches to the synthesis of unique polyribonucleotides.

The enzymatic polymerization by polynucleotide phosphorylase of 6-chloro-9-(beta-D-ribofuranosyl)purine 5'-diphosphate to poly(6-chloropurinylic acid) and its conversion to poly(6-thioninosinic acid) is described. The sulfur isostere of poly(I) was found not to form a complex with poly(C), but to form a self-association complex with a Tm around 295 degrees K. The sedimentation velocities, pKa and Tm values of the polymer have been examined under various conditions. A two (or more) stranded helical array is suggested as the most probable structure. Thermal loss of the thione chromophore was noted for poly- (S6I), S6IMP and S6I; the degradation product from S6I was shown to be inosine.

Alkaline Phosphatase