US2004132965A1PendingUtilityA1

Chemical reagents for formation of disulfide bonds in peptides

Assignee: UNIV CALIFORNIAPriority: May 26, 2000Filed: Oct 6, 2003Published: Jul 8, 2004
Est. expiryMay 26, 2020(expired)· nominal 20-yr term from priority
C40B 40/10C07K 1/1133B01J 2219/00277B01J 2219/00725C07K 1/006C07K 1/107
45
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Claims

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) 2 Cl 2 ] 2+ where en is ethylenediamine.

Claims

exact text as granted — not AI-modified
What is claimed is:  
     
         1 . A method of forming an intramolecular disulfide bond in a peptide, said method comprising: 
 contacting a peptide comprising at least two sulfhydryl (SH) groups with a compound having the formula:                          wherein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, I—, OH—, and RCO 2 — where R is an alkyl or substituted alkyl;    Pt is Pt(IV);    X 1 , X 2 , X 3 , and X 4  are ligands independently selected from the group consisting of a nitrogen ligand, an oxygen ligand, a phosphorous ligand, and a sulfur ligand;    i, k, m, and p are independently 0 or 1;    L 1 , L 2 , L 3 , and L 4  when present, are independently selected linkers.    
     
     
         2 . The method of  claim 1 , wherein said ligand is a nitrogen ligand selected from the group consisting of cyanide, ammonia, and an amine nitrogen.  
     
     
         3 . The method of  claim 1 , wherein X 1 , X 2 , X 3 , and X 4  are the same.  
     
     
         4 . The method of  claim 1 , wherein R 1  and R 2  are the same.  
     
     
         5 . The method of  claim 1 , wherein L 1  and L 2  are the same.  
     
     
         6 . The method of  claim 1 , wherein 
 i, k, m, and p are zero;    X 1 , X 2 , X 3 , and X 4  are cyanide or ammonia.    
     
     
         7 . The method of  claim 6 , wherein R 1  and R 2  are the same.  
     
     
         8 . The method of  claim 1 , wherein 
 i and k are 1    m and p are 0; and    L 1   i  and L 2   k  are linkers selected from the group consisting of alkyl linkers, substituted alkyl linkers, and aromatic linkers.    
     
     
         9 . The method of  claim 8 , wherein L 1   i  and L 2   k  are alkyl linkers comprising from 1 to 4 carbons.  
     
     
         10 . The method of  claim 9 , wherein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, and I—.  
     
     
         11 . The method of  claim 9 , wherein -X 1 -L 1 i-X 4 - and -X 2 -L 2   k -X 3 - are both: 
 —NH 2 CH 2 CH 2 NH 2 —.    
     
     
         12 . The The method of  claim 1 , wherein 
 i, k, m, and p are 1; and    X 1 -L 3 -X 2 -L 2 -X 3 -L 4 -X 4 -L 1  is H 2 NCH 2 CH 2 NHCH 2 CH 2 NHCH 2 CH 2 NH 2 .    
     
     
         13 . The method of  claim 1 , wherein said peptide ranges in length from about 2 amino acids to about 60 amino acids.  
     
     
         14 . The method of  claim 1 , wherein two amino acids that form a disulfide bond are adjacent amino acids.  
     
     
         15 . The method of  claim 1 , wherein two amino acids that form a disulfide bond are separated by no more than about 58 amino acids.  
     
     
         16 . The method of  claim 11 , wherein said peptide contains a methionine.  
     
     
         17 . The method of  claim 1 , wherein said contacting is at a pH ranging from about pH 0 to about pH 9.  
     
     
         18 . The method of  claim 1 , wherein said peptide is a chemically synthesized peptide.  
     
     
         19 . The method of  claim 1 , wherein said peptide is a chemically synthesized peptide bearing a protecting group.  
     
     
         20 . The method of  claim 19 , wherein said protecting group is an Fmoc or a tBoc.  
     
     
         21 . The method of  claim 1 , wherein said peptide is attached to a substrate.  
     
     
         22 . The method of  claim 1 , wherein X 1 , X 2 , X 3 , and X 4  are not cyanide.  
     
     
         23 . A solution comprising: 
 a peptide comprising at least two sulfhydryl groups; and    a compound having the formula:                          wherein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, I—, OH—, and RCO 2 — where R is an alkyl or substituted alkyl;    Pt is Pt(IV);    X 1 , X 2 , X 3 , and X 4  are ligands independently selected from the group consisting of a nitrogen ligand, an oxygen ligand, a phosphorous ligand, and a sulfur ligand;    i, k, m, and p are independently 0 or 1;    L 1 , L 2 , L 3 , and L when present, are independently selected linkers.    
     
     
         24 . The solution of  claim 23 , wherein said ligand is a nitrogen ligand selected from the group consisting of cyanide, ammonia, and an amine nitrogen.  
     
     
         25 . The solution of  claim 23 , wherein X 1 , X 2 , X 3 , and X 4  are the same.  
     
     
         26 . The solution of  claim 23 , wherein R 1  and R 2  are the same.  
     
     
         27 . The solution of  claim 23 , wherein L 1  and L 2  are the same.  
     
     
         28 . The solution of  claim 23 , wherein 
 i, k, m, and p are zero;    X 1 , X 2 , X 3 , and X 4  are cyanide or ammonia.    
     
     
         29 . The solution of  claim 28 , wherein R 1  and R 2  are the same.  
     
     
         30 . The solution of  claim 23 , wherein 
 i and k are 1;    m and p are zero; and    L 1  and L 2  are linkers selected from the group consisting of alkyl linkers, substituted alkyl linkers, and aromatic linkers.    
     
     
         31 . The method of  claim 30 , wherein L 1   i  and L 2   k  are alkyl linkers comprising from 1 to 4 carbons.  
     
     
         32 . The method of  claim 31 , wherein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, and I—.  
     
     
         33 . The method of  claim 31 , wherein -X 1 -L 1 i-X 1 - and -X 2 -L 2   k -X 3 - are both: 
 —NH 2 CH 2 CH 2 NH 2 —.    
     
     
         34 . The The method of  claim 1 , wherein 
 i, k, m, and p are 1; and    X 1 -L 3 -X 2 -L 2 -X 3 -L 4 -X 4 -L 1  is H 2 NCH 2 CH 2 NHCH 2 CH 2 NHCH 2 CH 2 NH 2 .    
     
     
         35 . The solution of  claim 30 , wherein L 1  and L 2  are alkyl linkers comprising from 1 to 4 carbons.  
     
     
         36 . The solution of  claim 35 , wherein R 1  and R 2  are the same and are selected from the group consisting of Cl—, Br—, and I—.  
     
     
         37 . The solution of  claim 35 , wherein -X 1 -L 1 -X 4 - and -X 2 -L 2 -X 3 - are both: 
 —NH 2 CH 2 CH 2 NH 2 —.    
     
     
         38 . The solution of  claim 23 , wherein said peptide ranges in length from about 2 amino acids to about 100 amino acids.  
     
     
         39 . The solution of  claim 23 , wherein two amino acids that form a disulfide bond are adjacent amino acids.  
     
     
         40 . The solution of  claim 23 , wherein two amino acids that form a disulfide bond are separated by no more than 60 amino acids.  
     
     
         41 . The solution of  claim 23 , wherein said peptide contains a methionine.  
     
     
         42 . The solution of  claim 23 , wherein said solution has a pH ranging from about pH 1 to about pH 9.  
     
     
         43 . The solution of  claim 23 , wherein said peptide is a chemically synthesized peptide.  
     
     
         44 . The solution of  claim 23 , wherein said peptide is a chemically synthesized peptide bearing a protecting group.  
     
     
         45 . The solution of  claim 23 , wherein said protecting group is an Fmoc or a tBoc.  
     
     
         46 . The solution of  claim 23 , wherein said peptide is attached to a substrate.  
     
     
         47 . A peptide synthesizer for the synthesis of a peptide having an intramolecular disulfide linkage, said peptide synthesizer comprising: 
 a plurality of vials, said vials containing amino acids derivatized for chemical peptide synthesis wherein at least one of said vials comprises an amino acid that, when fully deprotected, bears a sulfhydryl (SH) group; and    a vial comprising a reagent having the formula:                          herein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, I—, OH—, and RCO 2 — where R is an alkyl or substituted alkyl;    Pt is Pt(IV);    X 1 , X 2 , X 3 , and X 4  are independently selected from the group consisting of a nitrogen ligand, an oxygen ligand, a phosphorous ligand, and a sulfur ligand;    i, k, m, and p are independently 0 or 1;    L 1 , L 2 , L 3 , and L 4  when present, are independently selected linkers.    
     
     
         48 . The peptide synthesizer of  claim 47 , wherein said nitrogen ligand is selected from the group consisting of cyanide, ammonia, and an amine nitrogen.  
     
     
         49 . A method of chemically synthesizing a peptide comprising a disulfide linkage, said method comprising: 
 chemically coupling a plurality of amino acids to form a peptide comprising at least two sulfhydryl (SH) groups; and    contacting said peptide with a reagent having the formula:                          wherein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, I—, OH—, and RCO 2 — where R is an alkyl or substituted alkyl;    Pt is Pt(IV);    X 1 , X 2 , X 3 , and X 4  are ligands independently selected from the group consisting of a nitrogen ligand, an oxygen ligand, a phosphorous ligand, and a sulfur ligand;    i, k, m, and p are independently 0 or 1;    L 1 , L 2 , L 3 , and L 4  when present, are independently selected linkers.    
     
     
         50 . The method synthesizer of  claim 49 , wherein said ligand is a nitrogen ligand selected from the group consisting of cyanide, ammonia, and an amine nitrogen.  
     
     
         51 . The method of  claim 49 , wherein said contacting is in a buffer having a pH ranging from about pH 1 to about pH 9.  
     
     
         52 . A kit for forming an intramolecular disulfide bond in a peptide, said kit comprising: 
 a container containing a reagent having the formula:                          wherein R 1  and R 2  are independently selected from the group consisting of Cl—, Br—, I—, OH—, and RCO 2 — where R is an alkyl or substituted alkyl;    Pt is Pt(IV);    X 1 , X 2 , X 3 , and X 4  are ligands independently selected from the group consisting of a nitrogen ligand, an oxygen ligand, a phosphorous ligand, and a sulfur ligand;    i, k, m, and p are independently 0 or 1;    L 1 , L 2 , L 3 , and L 4  when present, are independently selected linkers.    
     
     
         53 . The kit of  claim 51 , wherein said ligand is a nitrogen ligand selected from the group consisting of cyanide, ammonia, and an amine nitrogen.  
     
     
         54 . The kit of  claim 51 , wherein said reagent is in a buffer at a pH ranging from about pH 1 to about pH 9.

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