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  Gamma-conopeptidesUSPTO Application #: 20060223984Title: Gamma-conopeptides Abstract: This invention relates to relatively short peptides about 25-40 residues in length, which are naturally available in minute amounts in the venom of the cone snails or analogs to the naturally available peptides, and which include three cyclizing disulfide linkages and one or more γcarboxyglutamate residues. More specifically, the present invention is directed to γ-conopeptides having the general formula I: Xaa1-Cys-Xaa2-Cys-Xaa3-Xaa4-Cys-Cys-Xaa5-Cys-Xaa6-Cys-Xaa7 (SEQ ID NO:1), as described herein; or having the general formula II: Xaa1-Cys-Xaa2-Cys-Xaa3-Xaa4-Cys-Cys-Xaa5-Xaa6-Cys-Xaa7-Cys-Xaa8 (SEQ ID NO:2), as defined herein; or having the general formula III: Xaa1-Cys-Xaa2-Cys-Xaa3-Xaa4-Xaa5-Cys-Cys-Ser-Asn-Ser-Cys-Asp-Xaa6-Cys-Xaa7 (SEQ ID NO:3), as described herein; or having the general formula IV: Xaa1-Cys-Xaa2-Cys-Xaa3-Xaa4-Xaa5-Cys-Cys-Ser-Asn-Ser-Cys-Asp-Xaa6-Cys-Xaa7 (SEQ ID NO:4), as described herein; or having the general formula V: Xaa1-Xaa2-Cys-Xaa3-Xaa4-Phe-Xaa5-Cys-Thr-Xaa6-Ser-Xaa7-Cys-Cys-Ser-Asn-Ser-Cys-Asp-Gln-Thr-Tyr-Cys-Xaa8-Leu-Xaa9 (SEQ ID NO:5), as described herein. The invention further relates to specific γ-conopeptides, specific pro-γ-conopeptides and nucleic acids encoding the pro-γ-conopeptides. The invention also includes pharmaceutically acceptable salts of the conopeptides. These conopeptides are useful as agonists of neuronal pacemaker calcium channels. (end of abstract)
Agent: Rothwell, Figg, Ernst & Manbeck, P.C. - Washington, DC, US Inventors: Michael M. Fainzilber, Karel S. Kits, Alma L. Burlingame, Baldomero M. Olivera, Craig Walker, Maren Watkins, Reshma Shetty, Lourdes J. Cruz, Julita Imperial, Clark Colledge USPTO Applicaton #: 20060223984 - Class: 530326000 (USPTO) Related Patent Categories: Chemistry: Natural Resins Or Derivatives; Peptides Or Proteins; Lignins Or Reaction Products Thereof, Peptides Of 3 To 100 Amino Acid Residues, 15 To 23 Amino Acid Residues In Defined Sequence The Patent Description & Claims data below is from USPTO Patent Application 20060223984. Brief Patent Description - Full Patent Description - Patent Application Claims
CROSS-REFERENCE TO RELATED APPLICATION [0001] The present application is a continuation of U.S. application Ser. No. 09/210,952, filed 15 Dec. 1998, which claims benefit of U.S. provisional patent application Ser. No. 60/069,706, filed 16 Dec. 1997, each of which is incorporated herein by reference, in its entirety. BACKGROUND OF THE INVENTION [0003] This invention relates to relatively short peptides about 25-40 residues in length, which are naturally available in minute amounts in the venom of the cone snails or analogs to the naturally available peptides, and which include three cyclizing disulfide linkages and one or more .gamma.-carboxyglutamate residues. [0004] The publications and other materials used herein to illuminate the background of the invention, and in particular, cases to provide additional details respecting the practice, are incorporated by reference, and for convenience are referenced in the following text by author and date and are listed alphabetically by author in the appended bibliography. [0005] Mollusks of the genus Conus produce a venom that enables them to carry out their unique predatory lifestyle. Prey are immobilized by the venom that is injected by means of a highly specialized venom apparatus, a disposable hollow tooth that functions both in the manner of a harpoon and a hypodermic needle. [0006] Few interactions between organisms are more striking than those between a venomous animal and its envenomated victim. Venom may be used as a primary weapon to capture prey or as a defense mechanism. Many of these venoms contain molecules directed to receptors and ion channels of neuromuscular systems. [0007] The predatory cone snails (Conus) have developed a unique biological strategy. Their venom contains relatively small peptides that are targeted to various neuromuscular receptors and may be equivalent in their pharmacological diversity to the alkaloids of plants or secondary metabolites of microorganisms. Many of these peptides are among the smallest nucleic acid-encoded translation products having defined conformations, and as such, they are somewhat unusual. Peptides in this size range normally equilibrate among many conformations. Proteins having a fixed conformation are generally much larger. [0008] The cone snails that produce these toxic peptides, which are generally referred to as conotoxins or conotoxin peptides, are a large genus of venomous gastropods comprising approximately 500 species. All cone snail species are predators that inject venom to capture prey, and the spectrum of animals that the genus as a whole can envenomate is broad. A wide variety of hunting strategies are used, however, every Conus species uses fundamentally the same basic pattern of envenomation. [0009] Several peptides isolated from Conus venoms have been characterized. These include the .alpha.-, .mu.- and .omega.-conotoxins which target nicotinic acetylcholine receptors, muscle sodium channels, and neuronal calcium channels, respectively (Olivera et al., 1985). A conotoxin, TxVIIA, containing a .gamma.-carboxyglutamate residued and three disulfide bonds has bee isolated (Fainzilber et al., 1991). Conopressins, which are vasopressin analogs, have also been identified (Cruz et al. 1987). In addition, peptides named conantokins have been isolated from Conus geographus and Conus tulipa (Mena et al., 1990; Haack et al., 1990). These peptides have unusual age-dependent physiological effects: they induce a sleep-like state in mice younger than two weeks and hyperactive behavior in mice older than 3 weeks (Haack et al., 1990). Recently, peptides named contryphans containing D-tryptophan or D-leucine residues have been isolated from Conus radiatus (U.S. Ser. No. 09/061,026), and bromo-tryptophan conopeptides have been isolated from Conus imperialis and Conus radiatus (U.S. Ser. No. 08/785,534). [0010] Ion channels are integral plasma membrane proteins responsible for electrical activity in excitable tissues. It has been recognized that slow inward currents can influence neuronal excitability via long-lasting depolarizations of the cell membrane (Llinas, 1988). The role of slow inward currents in generating endogenous bursting behavior has been recognized in molluscan neurons (Wilson & Wachtel, 1974; Eckert & Lux, 1976; Partridge et al., 1979), and more recently in some types of mammalian neurons (Lanthorn et al., 1984; Stafstrom et al., 1985; Llinas, 1988; Alonso & Llinas, 1989). Changes in the slow inward currents carried by such nonspecific cation channels may play a crucial role in bursting and pacemaker activities in a variety of excitable systems, ranging from mammalian heart muscle to molluscan neurons (Partridge & Swandulla, 1988; Hoehn et al., 1993; Kits & Mansvelder, 1966; van Soest & Kits, 1997). Slow inward currents are also believed to be important in generating epileptiform bursting in regions of the brain such as the hippocampus. [0011] It is desired to identify drugs which are useful for modulating slow inward cation channels in vertebrates involved in syndromes of clinical relevance, such as epileptic activity in hippocampus (Hoehn et al., 1993) and pacemaker potentials in heart muscle (Reuter, 1984). SUMMARY OF THE INVENTION [0012] This invention relates to relatively short peptides about 25-40 residues in length, which are naturally available in minute amounts in the venom of the cone snails or analogs to the naturally available peptides, and which include three cyclizing disulfide linkages and one or more .gamma.-carboxyglutamate residues. [0013] More specifically, the present invention is directed to conopeptides having the general formula I: [0014] Xaa.sub.1-Cys-Xaa.sub.2-Cys-Xaa.sub.3-Xaa.sub.4-Cys-Cys-Xaa.sub.5-Cys-Xaa- .sub.6-Cys-Xaa.sub.7 (SEQ ID NO:1), wherein Xaa.sub.1 is des-Xaa.sub.1 or a peptide having 1-6 amino acids; Xaa.sub.2 is a peptide having 5-6 amino acids; Xaa.sub.3 is a peptide having 4 amino acids; Xaa.sub.4 is Glu, .gamma.-Glu (.gamma.-carboxyglutamic acid; also referred to as Gla) or Gln; Xaa.sub.5 is a peptide having 3-4 amino acids; Xaa.sub.6 is a peptide having 3-6 amino acids; and Xaa.sub.7 is des-Xaa.sub.7 or a peptide having 2-9 amino acids, with the proviso that when Xaa.sub.1 is des-Xaa.sub.1, then Xaa.sub.5 is not the tripeptide Ser-Asp-Asn; general formula II: [0015] Xaa.sub.1-Cys-Xaa.sub.2-Cys-Xaa.sub.3-Xaa.sub.4-Cys-Cys-Xaa.sub.5-Xaa.sub- .6-Cys-Xaa.sub.7-Cys-Xaa.sub.8 (SEQ ID NO:2), wherein Xaa.sub.1 is des-Xaa.sub.1 or a peptide having 1-6 amino acids; Xaa.sub.2 is a peptide having 5-6 amino acids; Xaa.sub.3 is a peptide having 4 amino acids; Xaa.sub.4 is Glu, .gamma.-Glu or Gln; Xaa.sub.5 is Ser or Thr; Xaa.sub.6 is a peptide having 2-3 amino acids; Xaa.sub.7 is a peptide having 3-6 amino acids; and Xaa.sub.8 is des-Xaa.sub.8 or a peptide having 2-9 amino acids, with the proviso that when Xaa.sub.1 is des-Xaa.sub.1 and Xaa.sub.5 is Ser, then Xaa.sub.6 is not the dipeptide Asp-Asn; general formula III: Xaa.sub.1-Cys-Xaa.sub.2-Cys-Xaa.sub.3-Xaa.sub.4-Cys-Cys-Ser-Asn-Ser-Cys-A- sp-Xaa.sub.5-Cys-Xaa.sub.6 (SEQ ID NO:3), wherein Xaa.sub.1 is a peptide having 1-6 amino acids; Xaa.sub.2 is a hexapeptide; Xaa.sub.3 is a peptide having 4 amino acids; Xaa.sub.4 is Glu or .gamma.-Glu; Xaa.sub.5 is a tripeptide; and Xaa.sub.6 is a peptide having 7-9 amino acids; general formula IV: [0016] Xaa.sub.1-Cys-Xaa.sub.2-Cys-Xaa.sub.3-Xaa.sub.4-Xaa.sub.5-Cys-Cys-Ser-Asn- -Ser-Cys-Asp-Xaa.sub.6-Cys-Xaa.sub.7 (SEQ ID NO:4), wherein Xaa.sub.1 is a peptide having 1-6 amino acids; Xaa.sub.2 is a hexapeptide; Xaa.sub.3 is Ser or Thr; Xaa.sub.4 is a tripeptide; Xaa.sub.5 is Glu or .gamma.-Glu; Xaa.sub.6 is a tripeptide; and Xaa.sub.7 is a peptide having 7-9 amino acids; or general formula V: [0017] Xaa.sub.1-Xaa.sub.2-Cys-Xaa.sub.3-Xaa.sub.4-Phe-Xaa.sub.5-Cys-Thr-Xaa.sub- .6-Ser-Xaa.sub.7-Cys-Cys-Ser-Asn-Ser-Cys-Asp-Gln-Thr-Tyr-Cys-Xaa.sub.8-Leu- -Xaa.sub.9 (SEQ ID NO:5), wherein Xaa.sub.1 is des-Xaa.sub.1 or a dipeptide; Xaa.sub.2 is Asp, Glu or .gamma.-Glu; Xaa.sub.3 is a dipeptide; Xaa.sub.4 is Trp or 6-bromo-Trp; Xaa.sub.5 is a dipeptide; Xaa.sub.6 is a dipeptide; Xaa.sub.7 is Glu or .gamma.-Glu; Xaa.sub.8 is any amino acid; and, Xaa.sub.9 is a pentapeptide [0018] The amino acid or the amino acid residues of the peptides is an amino acid selected from the group consisting of natural, modified or non-natural amino acids. The disulfide bridges in the conopeptides of general formulas I-V (as well as the specific conopeptides described herein) are between the first and fourth cysteine residues, between the second and fifth cysteine residues and between the third and sixth cysteine residues. The C-terminal end may contain a carboxyl or amide group. The invention also includes pharmaceutically acceptable salts of the conopeptides. These conopeptides are useful for modulating slow inward cation channels in vertebrates involved in syndromes of clinical relevance, such as epileptic activity in hippocampus (Hoehn et al, 1993) and pacemaker potentials in heart muscle (Reuter, 1984). Thus, the conopeptides are useful as agonists of neuronal pacemaker cation channels. [0019] The invention further relates to the specific peptides: [0020] Asp-Cys-Thr-Ser-Xaa.sub.1-Phe-Gly-Arg-Cys-Thr-Val-Asn-Ser-Xaa.sub.2-Cys-C- ys-Ser-Asn-Ser-Cys-Asp-Gln-Thr-Tyr-Cys-Xaa.sub.2-Leu-Tyr-Ala-Phe-Xaa.sub.3- -Ser (SEQ ID NO:6) (PnVIIA), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or hydroxy-Pro (Hyp), preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably a free carboxyl group; [0021] Xaa.sub.1-Leu-Xaa.sub.2-Cys-Ser-Val-Xaa.sub.1-Phe-Ser-His-Cys-Thr-Lys-Asp- -Ser-Xaa.sub.2-Cys-Cys-Ser-Asn-Ser-Cys-Asp-Gln-Thr-Tyr-Cys-Thr-Leu-Met-Xaa- .sub.3-Xaa.sub.3-Asp-Xaa.sub.1 (SEQ ID NO:7) (Tx6.4), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or Hyp, preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably a free carboxyl group; [0022] Xaa.sub.1-Xaa.sub.1-Arg-Xaa.sub.1-Gly-Gly-Cys-Met-Ala-Xaa.sub.1-Phe-Gly-L- eu-Cys-Ser-Arg-Asp-Ser-Xaa.sub.2-Cys-Cys-Ser-Asn-Ser-Cys-Asp-Val-Thr-Arg-C- ys-Xaa.sub.2-Leu-Met-Xaa.sub.3-Phe-Xaa.sub.3-Xaa.sub.3-Asp-Xaa.sub.1 (SEQ ID NO:8) (Tx6.9), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or Hyp, preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably a free carboxyl group; [0023] Cys-Lys-Thr-Tyr-Ser-Lys-Tyr-Cys-Xaa.sub.2-Ala-Asp-Ser-Xaa.sub.2-Cys-Cys-T- hr-Xaa.sub.2-Gln-Cys-Val-Arg-Ser-Tyr-Cys-Thr-Leu-Phe (SEQ ID NO:9) (J010), wherein Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; and the C-terminus is a free carboxyl group or is amidated, preferably amidated; [0024] Asp-Xaa.sub.1-Xaa.sub.1-Asp-Asp-Gly-Cys-Ser-Val-Xaa.sub.1-Gly-Xaa.- sub.3-Cys-Thr-Val-Asn-Ala-Xaa.sub.2-Cys-Cys-Ser-Gly-Asp-Cys-His-Xaa.sub.2-- Thr-Cys-Ile-Phe-Gly-Xaa.sub.1-Xaa.sub.2-Val (SEQ ID NO:10) (Tx6.6), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or Hyp, preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably a free carboxyl group; [0025] Gly-Met-Xaa.sub.1-Gly-Xaa.sub.2-Cys-Lys-Asp-Gly-Leu-Thr-Thr-Cys-Leu-Ala-X- aa.sub.3-Ser-Xaa.sub.2-Cys-Cys-Ser-Xaa.sub.2-Asp-Cys-Xaa.sub.2-Gly-Ser-Cys- -Thr-Met-Xaa.sub.1 (SEQ ID NO:11) (Tx6.5), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or Hyp, preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably a free carboxyl group; [0026] Xaa.sub.2-Cys-Arg-Ala-Xaa.sub.1-Tyr-Ala-Xaa.sub.3-Cys-Ser-Xaa.sub.3-Gly-A- la-Gln-Cys-Cys-Ser-Leu-Leu-Met-Cys-Ser-Lys-Ala-Thr-Ser-Arg-Cys-Ile-Leu-Ala- -Leu (SEQ ID NO:12) (Gm6.7), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or Hyp, preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably a free carboxyl group; [0027] Asn-Gly-Gln-Cys-Xaa.sub.2-Asp-Val-Xaa.sub.1-Met-Xaa.sub.3-Cys-Thr-Ser-Asn- -Xaa.sub.1-Xaa.sub.2-Cys-Cys-Ser-Leu-Asp-Cys-Xaa.sub.2-Met-Tyr-Cys-Thr-Gln- -Ile (SEQ ID NO:13) (Mr6.1), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; Xaa.sub.3 is Pro or Hyp, preferably Hyp; and the C-terminus is a free carboxyl group or is amidated, preferably amidated; [0028] Cys-Gly-Gly-Xaa.sub.1-Ser-Thr-Tyr-Cys-Xaa.sub.2-Val-Asp-Xaa.sub.2-Xaa.sub- .2-Cys-Cys-Ser-Xaa.sub.2-Ser-Cys-Val-Arg-Ser-Tyr-Cys-Thr-Leu-Phe (SEQ ID NO:14) (Mr6.2), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; and the C-terminus is a free carboxyl group or is amidated, preferably amidated; [0029] Asn-Gly-Gly-Cys-Lys-Ala-Thr-Xaa.sub.1-Met-Ser-Cys-Ser-Ser-Gly-Xaa.sub.1-X- aa.sub.2 Cys-Cys-Ser-Met-Ser-Cys-Asp-Met-Try-Cys (SEQ ID NO:15) (Mr6.3), wherein Xaa.sub.1 is Trp or 6-bromo-Trp; Xaa.sub.2 is Glu or .gamma.-Glu, preferably .gamma.-Glu; and the C-terminus is a free carboxyl group or is amidated, preferably amidated. [0030] Finally, the invention further relates to the propeptide sequences for the above peptides and the DNA sequences coding for these propeptide sequences as described in further detail herein. SEQUENCE SUMMARY [0031] SEQ ID NO:1=.gamma.-conopeptides of general formula I; SEQ ID NO:2=.gamma.-conopeptides of general formula II; SEQ ID NO:3=.gamma.-conopeptides of general formula III; SEQ ID NO:4=.gamma.-conopeptides of general formula IV; SEQ ID NO:5=.gamma.-conopeptides of general formula V; SEQ ID NO:6=.gamma.-conopeptide corresponding to PnVIIA; SEQ ID NO:7=.gamma.-conopeptide corresponding to Tx6.4; SEQ ID NO:8=.gamma.-conopeptide corresponding to Tx6.9; SEQ ID NO:9=.gamma.-conopeptide corresponding to J010; SEQ ID NO:10=.gamma.-conopeptide corresponding to Tx6.6; SEQ ID NO:11=.gamma.-conopeptide corresponding to Tx6.5; SEQ ID NO:12=.gamma.-conopeptide corresponding to Gm6.7; SEQ ID NO:13=.gamma.-conopeptide corresponding to Mr6.1; SEQ ID NO:14=.gamma.-conopeptide corresponding to Mr6.2; SEQ ID NO:15=.gamma.-conopeptide corresponding to Mr6.3; SEQ ID NO:16=DNA encoding propeptide of Tx6.4; SEQ ID NO:17=propeptide of Tx6.4; SEQ ID NO:18=DNA encoding propeptide of Tx6.9; SEQ ID NO:19=propeptide of Tx6.9; SEQ ID NO:20=DNA encoding propeptide of J010; SEQ ID NO:21=propeptide of J010; SEQ ID NO:22=DNA encoding propeptide of Tx6.6; SEQ ID NO:23=propeptide of Tx6.6; SEQ ID NO:24=DNA encoding propeptide of Tx6.5; SEQ ID NO:25=propeptide of Tx6.5; SEQ ID NO:26=DNA encoding propeptide of Gm6.7; SEQ ID NO:27=propeptide of Gm6.7; SEQ ID NO:28=DNA encoding propeptide of Mr6.1; SEQ ID NO:29=propeptide of Mr6.1; SEQ ID NO:30=DNA encoding propeptide of Mr6.2; SEQ ID NO:31=propeptide of Mr6.2; SEQ ID NO:32=DNA encoding propeptide of Mr6.3; SEQ ID NO:33=propeptide of Mr6.3; SEQ ID NO:34=DNA encoding propeptide of Tx6.1; SEQ ID NO:35=propeptide of Tx6.1; SEQ ID NO:36=.gamma.-conopeptide corresponding to Tx6.1; SEQ ID NO:37=consensus sequence of .gamma.-conopeptides PnVIIA and Tx6.4; SEQ ID NO:38=degenerate probe for consensus sequence of .gamma.-conopeptides; SEQ ID NO:39=degenerate probe for consensus sequence of .gamma.-conopeptides; SEQ ID NO:40=consensus sequence of pro-.gamma.-conopeptides; SEQ ID NO:41=degenerate probe for consensus sequence of pro-.gamma.-conopeptides; SEQ ID NO:42=.gamma.-conopeptide PnVIIA; SEQ ID NO:43=.gamma.-conopeptide TxVIIA; SEQ ID NO:44=N-terminal tryptic peptide of .gamma.-conopeptide PnVIIA; SEQ ID NO:45=C-terminal tryptic peptide of .gamma.-conopeptide PnVIIA; SEQ ID NO:46=primer for isolating conopeptides from Conus textile cDNA library; SEQ ID NO:47=primer for isolating conopeptides from Conus textile cDNA library. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENT [0032] This invention relates to relatively short peptides about 25-40 residues in length, which are naturally available in minute amounts in the venom of the cone snails or analogs to the naturally available peptides, and which include three cyclizing disulfide linkages and one or more .gamma.-carboxyglutamate residues. [0033] More specifically, the present invention is directed to conopeptides having the general formulas I-V described above. The invention is also directed to the specific .gamma.-conopeptides PnVIIA, Tx6.4, Tx6.9, J010, Tx6.6, Tx6.5, Gm6.7, Mr6.1, Mr6.2 and Mr6.3, the sequences of which are described above. [0034] The invention is further directed to isolated nucleic acids which encode .gamma.-conopeptides, including the above and .gamma.-conopeptide Tx6.1, and to isolated propeptides encoded by the nucleic acids. This aspect of the present invention is set forth in Table 1. TABLE-US-00001 TABLE 1 Nucleic Acids and Propeptides of .gamma.-Conopeptides Nucleic Acid Propeptide SEQ .gamma.-Conopeptide SEQ ID NO: ID NO: Tx6.4 16 17 Tx6.9 18 19 J010 20 21 Tx6.6 22 23 Tx6.5 24 25 Gm6.7 26 27 Mr6.1 28 29 Mr6.2 30 31 Mr6.3 32 33 Tx6.1 34 35 The mature peptide sequence for Tx6.1 is LCX.sub.3DYTX.sub.2X.sub.3CSHAHX.sub.2CCSX.sub.1NCYNGHCT (SEQ ID NO: 36), wherein X.sub.1, X.sub.2 and X.sub.3 are as described for Xaa.sub.1, Xaa.sub.2 and Xaa.sub.3, respectively. The C-terminus is preferably amidated. Continue reading... Full patent description for Gamma-conopeptides Brief Patent Description - Full Patent Description - Patent Application Claims Click on the above for other options relating to this Gamma-conopeptides patent application. ###  How KEYWORD MONITOR works... a FREE service from FreshPatents1. Sign up (takes 30 seconds). 2. Fill in the keywords to be monitored. 3. Each week you receive an email with patent applications related to your keywords. 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