Abstract: A drug complex useful as a DDS compound, which is represented by the following formula: A-R—NH—Y—CH2—O—CO-Q, wherein A is a polymer as a drug carrier; R is a spacer, wherein the spacer is an amino acid or an oligopeptide comprising 2 to 8 amino acids; Y is phenylene group which may be substituted; and Q is a residue of a drug compound such as antineoplastic agents. The complex provides rapid and site-selective release of a drug compound such as antineoplastic or anti-inflammatory agents and surely exhibits expected efficacy.

Abstract: The invention provides a novel reductive alkylation method useful for selectively alkylating saccharide-amines of glycopeptide antibiotics.

Abstract: Compounds that modulate natural &bgr; amyloid peptide aggregation are provided. The modulators of the invention comprise a peptide, preferably based on a &bgr; amyloid peptide, that is comprised entirely of D-amino acids. Preferably, the peptide comprises 3-5 D-amino acid residues and includes at least two D-amino acid residues independently selected from the group consisting of D-leucine, D-phenylalanine and D-valine. In a particularly preferred embodiment, the peptide is a retro-inverso isomer of a &bgr; amyloid peptide, preferably a retro-inverso isomer of A&bgr;17-21. In certain embodiments, the peptide is modified at the amino-terminus, the carboxy-terminus, or both. Preferred amino-terminal modifying groups alkyl groups. Preferred carboxy-terminal modifying groups include an amide group, an acetate group, an alkyl amide group, an aryl amide group or a hydroxy group.

Abstract: Materials which are not themselves storage-stable at room temperature are made suitable for storage by mixing them with a carrier substance and spray drying the resulting mixture so as to form particles containing both the material and the carrier substance in which the carrier substance is in an amorphous, i.e. glassy or rubbery, state. Formation of such a composition greatly enhances stability. The material stored may be a biological material such as an enzyme, the components of a chemical reaction such as reagents for carrying out an assay, or even viable biological cells.

Abstract: A molecular conjugate is provided having the formula: wherein n is the conjugation number, P is a moiety of a carrier molecule such as a protein, R1 is a moiety of a biologically active molecule or its analogs, derivatives, salts or secondary amines, Z is —O— or —NH—, and Y is a straight or branched alkyl having 1 to 20 carbons optionally substituted with one or more phenyl, a cycloalkyl optionally substituted with one or more alkyl or phenyl, or an aromatic group optionally substituted with one or more alkyl, electron-withdrawing or electron-donating groups. Compounds and methods useful in producing such molecular conjugates are also provided, as well as methods of concentrating biologically active molecules in selected target cells of a patient that comprise administering to the patient a selected dose of such molecular conjugates.

Abstract: The present invention relates to conjugates for mediating a cell-specific, compartment-specific or membrane-specific to methods of active substances. The invention also relates to methods of preparing these conjugates as well as their use. The conjugates comprise: a transport mediator for the cell membrane, a cell-specific, compartment-specific or membrane-specific address protein or peptide, and an active substance to be transported.

Abstract: Compositions of the invention include composites comprising a biomaterial having compounds thereon with enhanced cell binding with respect to collagen. These composites are useful for soft and hard tissue repair or reconstruction and for in vitro uses. Suitable compounds with enhanced cell binding include synthetic peptides that mimic the conformation necessary for recognition and docking of collagen binding species (such as cell surface receptors for collagen and fibronectin) and have the amino acid residues -Ile-Ala- folded in a &bgr;-bend.

Abstract: Methods are described for conjugating radioiodinated non-metabolizable peptides to proteins and antibodies with improved yields and qualities of conjugates. Radioiodinated residualizing antibody conjugates comprising any aminopolycarboxylate-appended peptide, or any carbohydrate-appended peptide, are also provided. Additionally, methods are described for conjugating radioiodinated aminopolycarboxylates to proteins and antibodies, as well as for conjugating radioiodinated non-metabolizable carbohydrates to proteins and antibodies by a variety of chemical approaches. The instant radioiodinated residualizing antibody conjugates are particularly stable in vivo and are suitable for radioimmunodetection and radioimmunotherapy.

Abstract: The invention relates to a process for the conversion of echinocandin class of peptides to their C4-homotyrosine monodeoxy analogues, particularly mulundocandin to deoxymulundocandin, which consists of a single step selective reduction of C4-htyr (homotyrosine) hydroxyl group of echinocandins to their monodeoxy analogues under neutral conditions without prior protection/deprotection of the equally facile C5-Orn (ornithine) hydroxyl group and purification of the monodeoxy compound from the crude reaction mixture.

Abstract: The present invention concerns a process by which a misfold in an Fc fusion molecule can be prevented or corrected. In one embodiment, the process comprises (a) preparing a pharmacologically active compound comprising an Fc domain; (b) treating the fusion molecule with a copper (II) halide; and (c) isolating the treated fusion molecule. The pharmacologically active compound can be an antibody or a fusion molecule comprising a pharmacologically active domain and an Fc domain. The preferred copper (II) halide is CuCl2. The preferred concentration thereof is at least about 10 mM for fusion molecules prepared in E. coli; at least about 30 mM for fusion molecules prepared in CHO cells. The process can be employed with any number of pharmacologically active domains. Preferred pharmacologically active domains include OPG proteins, leptin proteins, soluble portions of TNF receptors (e.g., wherein the fusion molecule is etanercept), IL-1ra proteins, and TPO-mimetic peptides.

Abstract: A novel method for the determination of amino acids by HPLC using pre-column derivatization is described. In this procedure, the aminno acids are derivatized with 2-chlorobenzoxazole to yield highly fluroresent N-(2-benzoxazolyl)-amino acids (BOX-AAs) for detection at very high sensitivity. Derivatives can also be detected using conventional UV detection methods. The BOX-AAs can be separated on a C18 reversed phase column for quantitative estimation. This method can be used for the preparation of N-(2-benzoxazolyl)-amino acids in large amounts.

Abstract: Reagents and methods are provided for crosslinking and immobilizing biomolecules, drugs and synthetic polymers. The reagents possess (i) a thiol or amino reactive group; and (ii) a hydrazino or oxyamino moiety. Conjugates and immobilized biomolecules are also provided.

Abstract: Fluorinated alkyl compounds may be used as reaction intermediates or reaction products in polymerizing amino acid structures into peptides. Fluorinated methyl groups have been found to be particularly useful. A compound having a fluorinated methyl group such as that set forth below: wherein R is selected from the group consisting of: alkyls, hydrogen, aryls, aromatic compounds, amines, sulfur-containing alkyl groups, sulfur-containing aryl groups, and heterocyclic compounds may be utilized alone, or reacted in combination with other amino acids, to form a dipeptide, or polypeptide.

Abstract: The invention relates to an isolated, synthetic or recombinant &khgr;-conotoxin peptide having the ability to inhibit a neuronal amine transporter, nucleic acid molecules encoding all or part of such peptides, antibodies to such peptides and uses and methods of treatment involving them.

Abstract: The present invention relates to the ligand polypeptide for the human pituitary- and mouse pancreas-derived G protein-coupled receptor proteins. The ligand polypeptide or the DNA which codes for the ligand polypeptide can be used for (1) development of medicines such as pituitary function modulators, central nervious system function modulators, and pancreatic function modulators, and (2) development of receptor binding assay systems using the expression of recombinant receptor proteins and screening of pharmaceutical candidate compounds. In particular, by the receptor binding assay systems utilizing the expression of recombinant G protein-coupled receptor proteins in accordance with the invention, agonists and antagonists of G protein-coupled receptors which are specific to human and other warm-blooded animals can be screened and the agonists or antagonists obtained can be used as therapeutic and prophylactic agents for various diseases.

Abstract: A method for producing peptide salts, including reacting an acid addition salt of a basic starting peptide in the presence of a diluent in a mixed bed ion exchanger, with a mixture of an acid and a basic ion exchanger during the formation of a free basic peptide, and then separating the ion exchanger and then the free basic peptide, with an inorganic or organic acid, and then forming the desired acid addition salt of the peptide, and removing the diluent.

Abstract: A method for removing from a peptide the diketone of the methionine residue, and a method for manufacturing a peptide or salt thereof which does not possess an N-terminal methionine residue, characterized by having a peptide or salt thereof which possesses a diketone of the optionally oxidized N-terminal methionine residue react with 3,4-diaminobenzoic acid or a salt thereof in the presence of acetic acid and sodium formate, formic acid and sodium formate, or formic acid and sodium acetate.

Abstract: This invention relates to macromolecule modifiers containing biologically active drugs/biomolecules, or precursors thereof, and fluoroligomers; compositions comprising the macromolecules containing the drugs and fluoroligomers in admixture with polymers, particularly biomedical polymers; articles made from the admixtures, particularly medical devices.

Abstract: The present invention broadly relates to chemical modification of biologically active proteins or analogs thereof. More specifically, the present invention describes novel methods for site-specific chemical modification of various proteins, and resultant compositions having improved biocompatibility and bioactivity.

Abstract: Novel cyclodepsipeptide intermediates have been prepared from the A21978 complex and used to synthesize new lipodepsipeptide antibiotics. The three intermediates can be readily derivatized to give new families of antibiotics that have potent antibacterial activity against gram positive bacteria.

Abstract: In this application is described substrates for high-throughput assays of clostridial neurotoxin proteolytic activities. Two types of substrates are described for use in assays for the proteolytic activities of clostridial neurotoxins: (1) modified peptides or proteins that can serve as FRET substrates and (2) modified peptides or proteins that can serve as immobilized substrates. In both types a fluorescent molecules is present in the substrate, eliminating the requirement for the addition of a fluorigenic reagent. The assays described can be readily adapted for use in automated or robotic systems.

Abstract: A method for producing a S-nitrosylated species is provided. The method comprises: (a) providing a deoxygenated, alkaline aqueous solution comprising a thiol and a nitrite-bearing species; (b) acidifying the solution by adding acid to the solution while concurrently mixing the solution (e.g., by vigorously stirring the solution) to produce the S-nitrosylated species; and (c) isolating the S-nitrosylated species. The nitrite-bearing species can be, for example, an inorganic nitrite, such as an alkali metal nitrite, or an organic nitrite, such as an alkyl nitrite (e.g., ethyl nitrite, amyl nitrite, isobutyl nitrite or t-butyl nitrite). The thiol is preferably a thiol-containing polysaccharide, a thiol-containing lipoprotein, a thiol-containing amino acid or a thiol-containing protein, and more preferably a thiol-containing polysaccharide such as thiolated cyclodextrin. In many preferred embodiments, the S-nitrosylated species is insoluble in the acidified solution, precipitating upon formation.

Abstract: Methods of preparing peptide linked oligomeric compounds are provided. The method is useful for preparing larger scale amounts of peptide linked oligomeric compounds. More particularly, the synthesis of peptide linked oligomeric compounds is performed without the problems of aggregation associated with electrostatic interactions. The present method describes using equimolar amounts of oligomeric compounds and peptide reagents providing for an increase in overall efficiency.

Abstract: Conjugates containing a targeting ligand, such as an antibody, a therapeutically active drug and a branched peptide linker. The branched peptide linker contains two or more amino acid moieties that provide an enzyme cleavage site. The number of drugs capable of being bonded to the branched linkers varies by a factor of two for each generation of branching.

Abstract: A method of separating compounds that includes the steps of: tagging at least a first organic compound with a first tagging moiety to result in a first tagged compound; tagging at least a second organic compound with a second tagging moiety different from the first tagging moiety to result in a second tagged compound; and separating the first tagged compound from a mixture including the second tagged compound using a separation technique based upon differences between the first tagging moiety and the second tagging moiety. The present invention also provides a method for carrying out a chemical reaction including the steps of: tagging a plurality of compounds with different tagging moieties to create tagged compounds, conducting at least one chemical reaction on a mixture of the tagged compounds to produce a mixture of tagged products, and separating the mixture of tagged products by a separation technique based upon differences in the tagging moieties.

Abstract: This invention relates generally to dipeptides and tripeptides and to methods for pharmaceutical treatment of mammals using analogs of such dipeptides and tripeptides. More specifically, the invention relates to tripeptides and their analogs, to pharmaceutical compositions containing such dipeptides and tripeptides and to methods of treatment of mammals using such dipeptides and tripeptides. In addition, the invention relates to methods of treatment of mammals using such dipeptides and tripeptides for control of appetite, blood pressure, cardiovascular response, libido, and circadian rhythm.

Abstract: The present invention relates to compositions comprised of a peptide ligand or derivatives thereof that are capable of specific binding to the high affinity receptor-1 of vascular endothelial growth factor (VEGF) and structure similar receptors. The invention further provides a peptide ligand or derivatives thereof that are capable of inhibiting angiogenesis induced by VEGF. The present invention also provides a method for treatment or diagnosis of disease associated with angiogenesis in a patient in need of therapy comprising administering to the patient an effective amount of the pharmaceutical composition of the present invention and a pharmaceutical acceptable carrier.

Abstract: Polycation bioconjugates and a method for producing them. The polycations are capable of transporting active substances of different types. The polycations function as carrier molecules that transport enhancer molecules, thereby enhancing the biological effectiveness of the transported molecules. The polycation bioconjugates of the present invention may inhibit malignant cell proliferation, possess antimicrobial effect, or be configured for gene transport.

Abstract: Polyamide conjugates comprising either (a) a xenoantigenic group; or (b) a biologically active group and a macromolecular, macro- or microscopic entity; bound to a polyamide backbone, processes for their preparation and the use of these conjugates in therapeutic compositions.

Abstract: A compound of Formula I, providing tetrapartate prodrugs is provided wherein: L1 is a bifunctional linking moiety; D is a moiety that is a leaving group, or a residue of a compound to be delivered into a cell; Z is covalently linked to [D]y, wherein Z is selected from the group consisting of: a moiety that is actively transported into a target cell, a hydrophobic moiety, and combinations thereof, Y1, Y2, Y3 and Y4 are each independently O, S, or NR12; R11 is a mono- or divalent polymer residue; R1, R4, R9, R10 and R12 are independently selected from the group consisting of hydrogen, C1-6 alkyls, C3-12 branched alkyls, C3-8 cycloalkyls, C1-6 substituted alkyls, C3-8 substituted cycloalkyls, aryls, substituted aryls, aralkyls, C1-6 heteroalkyls and substituted C1-6 heteroalkyls; R2, R3, R5 and R6 are independently selected from the group consisting of hydrogen, C1-6 alkyls, C1-6 alkoxy, phenoxy, C1-8 heteroalkyls, C1-8 heteroalkoxy, substituted C1-6 alkyls, C3-8 cycloalkyls, C

Abstract: A composition comprising a polypeptide and an active agent covalently attached to the polypeptide. Also provided is a method for delivery of an active agent to a patient comprising administering to the patient a composition comprising a polypeptide and an active agent covalently attached to the polypeptide. Also provided is a method for protecting an active agent from degradation comprising covalently attaching the active agent to a polypeptide. Also provided is a method for controlling release of an active agent from a composition comprising covalently attaching the active agent to the polypeptide.

Abstract: Compounds having the following peptide sequence: X Leu Y, wherein X is H or Ala or Leu-Ser-Ala, Y is OH or peptide sequence having from 1 to 10 amino acids, with the terminal carboxy end being amidified by a NH2 group, or esterified by a substituted or non-substituted hydrocarbyloxy, with the proviso that X and Y are not simultaneously H and OH, respectively, The invention also concerns the corresponding compounds wherein the peptide binding group —CO—NH— is replaced by a binding group resisting protease enzymatic degradation, or wherein the peptide backbone comprises one or more intercalated groups making the peptide binding resistant to enzymatic degradation. Also described are compounds comprising a grouping whose spatial structure is substantially identical to that of a peptide of the sequence X-Leu-Y wherein X and Y have the above-mentioned definition.

Abstract: A mixture of conjugates in which each conjugate in the mixture comprises a calcitonin drug coupled to an oligomer that includes a polyalkylene glycol moiety is disclosed. The mixture may lower serum calcium levels in a subject by 10, 15 or even 20 percent or more. Moreover, the mixture may be more effective at surviving an in vitro model of intestinal digestion than non-conjugated calcitonin. Furthermore, the mixture may exhibit a higher bioavailability than non-conjugated calcitonin.

Abstract: Novel peptide dimers are provided that bind and activate the erythropoietin receptor (EPO-R) or otherwise act as an EPO agonist. The novel compounds have a first peptide chain R1 and a second peptide chain R2, wherein R1 and R2 may be the same or different, and are linked through a linking moiety. R1 is approximately 10 to 40 amino acid residues in length and comprises the sequence X3X4X5GPX6TX7X8X9 (SEQ ID NO: 1) wherein X3 is C or Hoc, X4 is R, H, L or W, X5 is M, F, I or nor-leucine (J), X6 is any one of the 20 genetically coded L-amino acids or J, X7 is W, 1-naphthylalanine (B) or 2-naphthylalanine (U), X8 is D, E, 1, L or V, and X9 is C or Hoc. Similarly, R2 comprises the sequence X′3X′4X′5GPX′6TX′7X′8X′9 (SEQ ID NO: 2) wherein X′3 is C or Hoc, X′4 is R, H, L or W, X′5 is M, F, I or J, X′6 is any one of the 20 genetically coded L-amino acids or J, X′7 is W, B or U, X8′ is D, E, I, L or V, and X′9 is C or Hoc.

Abstract: Novel oligopeptides comprising a sequence derived by a computer program are provided for use in inhibiting cytotoxic activity of lymphocytic cells, inhibiting the production of inflammatory cytokines and inflammatory responses associated with those cytokines, inhibiting the activity of heme-containing enzymes and delaying the onset of an autoimmune disease in a mammal at risk of developing the disease. By combining the subject compositions with mixtures of cells comprising lymphocytic cells and cells which would otherwise activate the lymphocytic cells, lysis of the target cells can be substantially inhibited. The oligopeptides may be joined to a wide variety of other groups or compounds for varying the activity of the subject compositions.

Abstract: Polypeptides which increase or promote mammalian bone growth, related nucleotide sequences, antibodies, diagnostic kits and treatments. Subsequences of the polypeptide (SEQ ID NO:2)Asp Ser Asp Leu Tyr Ala Glu Leu Arg Cys Met Cys Ile Lys Thr Thr Ser Gly Ile His Pro Lys Asn Ile Gln Ser Leu Glu Val Ile Gly Lys Gly Thr His Cys Asn Gln Val Glu Val Ile Ala Thr Leu Lys Asp Gly Arg Lys Ile Cys Leu Asp Pro Asp Ala Pro Arg Ile Lys Lys Ile Val Gln Lys Lys Leu Ala Gly Asp Glu Ser Ala Asp have been shown to promote growth. Subsequences include (SEQ ID NO:11) Asp Ser Asp Leu Tyr Ala Glu Leu Arg Cys Met Cys Ile Lys Thr Thr Ser Gly Ile His Pro Lys Asn Ile Gln Ser (SEQ ID NO:12); Ile Lys Thr Thr Ser Gly Ile His Pro Lys Asn Ile Glu Ser (SEQ ID NO:13); Cys Met Cys Ile Lys Thr Thr Ser Gly Ile His Pro Lys Asn Ile Gln Ser and (SEQ ID NO:19) TTSGIHPK.

Abstract: The present invention provides peptide analogs and peptide mimetics that inhibit pleated sheet formation in amyloid &bgr;-peptide, pharmaceutical compositions thereof and their therapeutic use. The inhibitory peptides possess activity as inhibitors in the formation of amyloid-like deposits and are useful in the treatment of Alzheimer's Disease.

Abstract: Compounds that modulate natural &bgr; amyloid peptide aggregation are provided. The modulators of the invention comprise a peptide, preferably based on a &bgr; amyloid peptide, that is comprised entirely of D-amino acids. Preferably, the peptide comprises 3-5 D-amino acid residues and includes at least two D-amino acid residues independently selected from the group consisting of D-leucine, D-phenylalanine and D-valine. In a particularly preferred embodiment, the peptide is a retro-inverso isomer of a &bgr; amyloid peptide, preferably a retro-inverso isomer of A&bgr;17-21. In certain embodiments, the peptide is modified at the amino-terminus, the carboxy-terminus, or both. Preferred amino-terminal modifying groups include cyclic, heterocyclic, polycyclic and branched alkyl groups. Preferred carboxy-terminal modifying groups include an amide group, an alkyl amide group, an aryl amide group or a hydroxy group.

Abstract: This invention pertains to the discovery of a class of reagents that effectively form intramolecular disulfide bonds in peptides. Intermolecular disulfide linkage formation is low or essentially non-existent. In addition, preferred reagents of this invention are relatively mild and do not oxidize “vulnerable” residues in the subject peptide(s). In addition the reagents and reaction products are safe and essentially non-toxic. One particularly preferred reagent is [Pt(en)2Cl2]2+ where en is ethylenediamine.

Abstract: A method is presented for the preparation and use of fluorogenic peptide substrates that allows for the configuration of general substrate libraries to rapidly identify the primary and extended specificity of enzymes, such as proteases. The substrates contain a fluorogenic-leaving group, such as 7-amino-4-carbamoylmethyl-coumarin (ACC). Substrates incorporating the ACC leaving group show comparable kinetic profiles as those with the traditionally used 7-amino-4-methyl-coumarin (AMC) leaving group. The bifunctional nature of ACC allows for the efficient production of single substrates and substrate libraries using solid-phase synthesis techniques. The approximately 3-fold increased quantum yield of ACC over AMC permits reduction in enzyme and substrate concentrations. As a consequence, a greater number of substrates can be tolerated in a single assay, thus enabling an increase in the diversity space of the library.

Abstract: Disulfide proteins showed mitigated allergenicity and increased digestibility by pepsin following reduction by thioredoxin. The sulfhydryl groups newly formed on reduction by thioredoxin (at 4° C.) or dithiothreitol (DTT) (at 55° C.) were blocked with a physiological disulfide, such as cystamine or oxidized glutathione (GSSG) to obtain stable forms of the disarmed allergen. When derivatized with cystamine, BLG was separated from its oxidized and reduced forms on non-reducing SDS-PAGE and appeared to lack sulfhydryl groups. Although less effective GSSG, gave similar results. Allergenicity of the two derivatives was compared with that of the oxidized, reduced and reoxidized forms of BLG by skin testing dogs from a colony sensitized to cow's milk. Both the cystamine and GSSG derivatized BLG showed decreased allergenicity and increased sensitivity to pepsin as compared to controls. The reoxidized form resembled the derivatives in having lower allergenicity.

Abstract: An antibacterial &bgr;-peptide having the following formula: wherein R1 is H, an alkyl group including 1-4 carbon atoms, phenyl, heteroaryl, or an alkyl-aryl; R2 is an amine-containing alkyl group having the formula —(CH2)mNH2, wherein m=1, 2, 3, 4, or 5, (CH2)xNHC═NHNH2 wherein x is 1, 2, 3, 4, or 5, a pyridyl, an alkylpryidyl, an amidine-substituted benzyl, a phenyl group, or a cyclic amidine; R3 is H, an alkyl group including 1-4 carbon atoms, phenyl, heteroaryl, or an alkyl-aryl; X is —NH2, —OH, —NHR, or OR where R is alkyl, aryl or acyl groups either free or polymer-supported, a carboxamide, a substituted carboxamide, or a polymer; Y is H, an alkyl group, an acyl group, an acyl-terminated polymer, a sulphonamide, an ether, a urea, a urethane, or a polymer; and n is 2, 3, 4, 5, 6, or 7.

Abstract: This invention relates to radiolabeled peptides and methods for producing such peptides. Specifically, the invention relates to peptides, methods and kits for making such peptides, and methods for using such peptides to image sites in a mammalian body labeled with technetium-99m (Tc-99m) via (Tc-99m) binding moieties. In particular, the peptide reagents of the invention are covalently linked to a polyvalent linker moiety, so that the polyvalent linker moiety is covalently linked to a multiplicity of the specific-binding peptides, and the Tc-99m binding moieties are covalently linked to a plurality of the specific-binding peptides, the polyvalent linker moiety, or to both the specific-binding peptides and the polyvalent linker moiety.

Abstract: A homogeneous polyoxime composition is provided, in which the polyoxime molecules present comprise a first organic baseplate molecule, which is a polypeptide, wherein the baseplate molecule is linked to at least two second organic molecules, which may be the same or different from one another. In the compositions, the linkages between the baseplate and said organic molecules are oxime linkages formed by reaction of an orthogonal reactive group on each the organic molecules with a complementary orthogonal reactive group on the baseplate.

Abstract: This invention provides novel peptides that ameliorate one or more symptoms of atherosclerosis. The peptides are highly stable and readily administered via an oral route.

Abstract: The solvent accessible reduced carbon atoms in a molecule of interest are labeled with heavy hydrogen. The carbon atoms are labeled under anaerobic, aqueous conditions by exposing the molecule of interest to a hydrogen atom abstractor in the presence of a heavy hydrogen source and a heavy hydrogen donor. If the hydrogen atom abstractor is hydroxyl radical, an electron scavenger source is provided. Optionally, an internal reference is provided to facilitate experimental reproducibility.

Abstract: A method of identifying a ligand for a second binding site (5) on a biological substrate (1) is disclosed. The method comprises determining the effect of a candidate compound (9) on the binding of a probe compound (2) which binds to a first binding site (3) on the biological substrate in the presence of a first multibinding compound (4) which binds to the first (3) and second (5) binding sites on the biological substrate (1).

Abstract: Multivalent immunogenic molecules comprise a carrier molecule containing at least one functional T-cell epitope and multiple different carbonhydrate fragments each linked to the carrier molecule and each containing at least one functional B-cell epitope. The carrier molecule inparts enhanced immunogenicity to the multiple carbohydrate fragments. The carbohydrate fragments may be capsular oligosaccharide fragments from Streptococcus pneumoniae which may be serotypes (1, 4, 5, 6B, 9V, 14, 18C, 19F or 23F), or Neisseria meningitidis, which may be serotype (A, B, C) W-135 or Y. Such oligosaccharide fragments may be sized from about 2 to about 5 kDa. Alternatively, the carbohydrate fragments may be fragments of carbohydrate-based tumor antigens, such as Globo H, LeY or STn. The multivalent molecules may be produced by random conjugation or site-directed conjugation of the carbohydrate fragments to the carrier molecule.

Abstract: The present invention is directed toward a method for preparing and purifying a conjugate of a radioiodinated aminopolycarboxylate-appended peptide and a targeting agent. The method involves (A) providing a solution comprising (i) unbound radioiodine (ii) a radioiodinated aminopolycarboxylate-appended peptide that is not conjugated to a targeting agent (iii) and a radioiodinated aminopolycarboxylate-appended peptide that is conjugated to the targeting agent; (B) contacting the solution with an anion-exchange resin; and (C) passing the anion-exchange resin and solution together through a filter capable of trapping anion-exchange resin particles.

Abstract: The solvent accessible reduced carbon atoms in a molecule of interest are labeled with heavy hydrogen. The carbon atoms are labeled under anaerobic, aqueous conditions by exposing the molecule of interest to a hydrogen atom abstractor in the presence of a heavy hydrogen source and a heavy hydrogen donor. If the hydrogen atom abstractor is hydroxyl radical, an electron scavenger source is provided. Optionally, an internal reference is provided to facilitate experimental reproducibility.