Abstract: The use of spider venom, molecules or synthetic analogs thereof for skin whitening. Also, compositions that include spider venom, molecules or synthetic analogs thereof for skin whitening/depigmenting, and a non-therapeutic method for whitening human skin that includes topically applying an effective amount on human skin of the composition.

Abstract: The invention relates to antibodies that bind to adrenomedullin and to proteins forming adrenomedullin receptors and to the uses thereof as drugs.

Abstract: The use of spider venom, molecules or synthetic analogs thereof for skin whitening. Also, compositions that include spider venom, molecules or synthetic analogs thereof for skin whitening/depigmenting, and a non-therapeutic method for whitening human skin that includes topically applying an effective amount on human skin of the composition.

Abstract: The invention relates to antibodies binding to the proteins forming adrenomedullin receptors, and to the uses thereof as a drug.

Abstract: The present invention relates to a method for monitoring the tumor growth of an androgen-independent prostate cancer in a subject, by determining the amount of at least one adrenomedullin receptor and optionally adrenomedullin in a prostate cancer cell obtained from said subject. The present invention also relates to a pharmaceutical composition comprising an anti-adrenomedullin antagonist antibody and/or at least one anti-adrenomedullin receptor antagonist antibody for treating an androgen-independent prostate cancer.

Abstract: The invention relates to antibodies that bind to adrenomedullin and to proteins forming adrenomedullin receptors and to the uses thereof as drugs.

Abstract: The invention relates to antibodies binding to the proteins forming adrenomedullin receptors, and to the uses thereof as a drug.

Abstract: Derivatives of Maurotoxin (MTX) in which the native disulfide bridge pattern (Cys3-Cys24, Cys9-Cys29, Cys19, Cys31-Cys34) has been disrupted are useful for the treatment of pathologies associated with dysfunctioning and/or activation of Ca2+-activated and/or voltage-gated K+ channel subtypes, such as IKCa1 or Kv1.2. In one group of derivatives, one or two of the amino acid residues of maurotoxin have been replaced by different amino acid residues resulting in the disulfide bridge pattern being changed to Cys3-Cys24, Cys9-Cys29, Cys13-Cys31, Cys19-Cys34. Exemplary substitutions include the Arg residue at position 14 and/or the Lys residue at position 15 replaced by a Gln residue and the Gly residue at position 33 replaced by an Ala residue. Pi1 and HsTx1 derivatives with disrupted native disulfide bridge patterns are similarly useful.

Abstract: Derivatives of Maurotoxin (MTX) in which the native disulfide bridge pattern (Cys3-Cys24, Cys9-Cys29, Cys19, Cys31-Cys34) has been disrupted are useful for the treatment of pathologies associated with dysfunctioning and/or activation of Ca2+-activated and/or voltage-gated K+ channel subtypes, such as IKCa1 or Kv1.2. One preferred group of derivatives is that in which one or more of the Cys residues have been replaced with ?-aminobutyrate (Abu) residues, thus breaking one or more of the four disulphide bridges. Within this group, the preferred derivative is that in which the Cys residues at position 9, 19, 29 and 34 have been replaced with a ?-aminobutyrate residues.

Abstract: Maurocalcine, a novel toxin isolated from the venom of the Tunisian chactidae scorpion Scorpio maurus palmatus, has the amino acid sequence GDCLPHLKLCKENKDCCSKKCKRRGTNIEKRCR (SEQ. ID. No. 1). It potently and reversibly modifies channel gating behaviour of type 1 ryanodine receptor (RyR1) by inducing prominent subconductance behavior. Maurocalcine and its bioactive structural analogues—preferably those containing the KKCKRR motif corresponding to part of the II-III loop of the alpha1S subunit of the voltage-dependent skeletal muscle calcium channel dihydropyridine receptor—appear to possess a therapeutic potential, notably as candidate immuno-suppressive drugs, and for the treatment of pathologies in humans that may involve a dysfunction of calcium channels.

Abstract: Multiple branch peptide constructions formed from peptide-branches derived from the envelope transmembrane glycoprotein gp41 of HIV, and including the consensus sequence RQGY preceded by 0 to 4 amino acid residues and succeeded by 0 to 4 amino acid residues, most preferably RQGYS, show increased receptor affinity and prevent cell-to-cell fusion. They have a direct virostatic effect. Because they present the same peptide sequence several times, these MBPCs are able to neutralize in vitro the different steps of virus envelope/cell membrane fusion, and infected cell membrane/uninfected cell membrane fusion of several strains of HIV-1 and HIV-2. These results open a potential use in treatment of HIV infection.

Abstract: The activity and cell membrane affinity of certain antiviral multiple branch peptide constructions, including those known from WO 95/07929, WO 98/29443 and WO 03/95479, can be improved by bonding to the C-end of the peptide a terminator which is either (a) an ?-amino-fatty acid having from 4 to 10 carbon atoms and from 0 to 2 carbon-carbon double bonds or (b) a peptidic cell membrane penetrating agent. The improvement is so marked that in some cases the number of branches can be reduced, sometimes to a single branch, and/or that the branches may be shortened. The preferred ?-amino-fatty acids are ?-aminobutyric acid, ?-aminovaleric acid and ?-aminocaproic acid. The peptidic cell membrane penetrating agent is suitably a TAT-derived peptide, penetratin® or Kpam.

Abstract: Multiple branch peptide constructions formed from peptide-branches derived from the envelope transmembrane glycoprotein gp41 of HIV, and including the consensus sequence RQGY preceded by 0 to 4 amino acid residues and succeeded by 0 to 4 amino acid residues, most preferably RQGYS, show increased receptor affinity and prevent cell-to-cell fusion. They have a direct virostatic effect. Because they present the same peptide sequence several times, these MBPCs are able to neutralize in vitro the different steps of virus envelope/cell membrane fusion, and infected cell membrane/uninfected cell membrane fusion of several strains of HIV-1 and HIV-2. These results open a potential use in treatment of HIV infection.

Abstract: Derivatives of Maurotoxin (MTX) in which the native disulfide bridge pattern (Cys3-Cys24, Cys9-Cys29, Cys19, Cys31-Cys34) has been disrupted are useful for the treatment of pathologies associated with dysfunctioning and/or activation of Ca2+-activated and/or voltage-gated K+ channel subtypes, such as IKCa1 or Kv1.2. One preferred group of derivatives is that in which one or more of the Cys residues have been replaced with ?-aminobutyrate (Abu) residues, thus breaking one or more of the four disulphide bridges. Within this group, the preferred derivative is that in which the Cys residues at position 9, 19, 29 and 34 have been replaced with a ?-aminobutyrate residues.

Abstract: Maurocalcine, a novel toxin isolated from the venom of the Tunisian chactidae scorpion Scorpio maurus palmatus, has the amino acid sequence GDCLPHLKLCKENKDCCSKKCKRRGTNIEKRCR (SEQ. ID. No. 1). It potently and reversibly modifies channel gating behaviour of type 1 ryanodine receptor (RyR1) by inducing prominent subconductance behavior. Maurocalcine and its bioactive structural analogues—preferably those containing the KKCKRR motif corresponding to part of the II-III loop of the alpha1S subunit of the voltage-dependent skeletal muscle calcium channel dihydropyridine receptor—appear to possess a therapeutic potential, notably as candidate immuno-suppressive drugs, and for the treatment of pathologies in humans that may involve a dysfunction of calcium channels.

Abstract: Multiple branch peptide constructions formed from peptides derived from the envelope transmembrane glycoprotein gp41 of HIV, and including the consensus sequence RQGY preceded by 0 to 4 amino acid residues and succeeded by 2 to 4 amino acid residues, most preferably RQGYSPL, show increased receptor affinity and prevent cell-to-cell fusion. They have a direct virostatic effect. Because they present the same peptide sequence several times, these MBPCs are able to neutralize in vitro the different steps of virus envelope/cell membrane fusion, and infected cell membrane/uninfected cell membrane fusion of several strains of HIV-1 and HIV-2. These results open a potential use in treatment of HIV infection.

Abstract: The present invention teaches multiple branch peptide constructions (MBPCs) formed from a core matrix to which is attached peptides derived from the V3 loop of the envelope glycoprotein of HIV-1, and including the amino acid sequence GPGR (SEQ ID NO: 5), preferably in the form GPGRAF, but which peptides preferably are free of the amino acid sequences IGPGR (SEQ ID NO: 1) or IXXGPGR (SEQ ID NO: 3), where X is an amino acid residue, and the use of such MBPCs as a therapy against HIV. The MBPCs prevent virus/cell infection and cell-to-cell virus transmission between CD4.sup.+ cells and HIV without hindering the immunogenic role of the CD4.sup.+ cells. Moreover, the MBPCs are effective in blockading both CD4 receptors on lymphocytes and macrophages and GalCer receptors on colon epithelial cells. These MBPCs are not immunogenic nor toxic at doses of their intended use (<[10.sup.-3 M]), thus allowing for them to be used therapeutically.