Abstract: A process for the production of pramlintide, a 37-mer peptide, is provided. The synthesis provides a high yield synthesis of the peptide in relatively pure form. Further purification can be achieved by preparative HPLC.

Abstract: The present invention relates to an improved process for the large scale synthesis of cyclic heptapeptide using Fmoc solid phase synthesis technique. The described process assembles the peptide on a solid support resin by coupling to one another by peptide bonds to obtain a peptide wherein the coupling of cysteine to the resin employs a combination of solvents to reduce cysteine racemization. The process described relates to the use of C1-C4 alcohols as total substitute to organic nitriles thus making the process cost effective, non-toxic and eco-friendly.

Abstract: The present invention relates to a process for improving pegylation reaction yield of r-metHuG-CSF comprising conjugating r-metHuG-CSF to a PEG aldehyde at a free amine moiety at the N terminal end on the G-CSF in presence of a reducing agent in a pegylation buffer solution comprising a polyol having the formula CnH2n+2On where n is from 3 to 6, or a carbohydrate, or a derivative thereof wherein the concentration of said polyol or carbohydrate or derivative thereof is in the range of 0.1% to 10% w/w.

Abstract: A process for the production of pramlintide, a 37-mer peptide, is provided. The synthesis provides a high yield synthesis of the peptide in relatively pure form. Further purification can be achieved by preparative HPLC.

Abstract: This invention relates a process for preparing octreotide and derivatives thereof. The starting material, Cys(Trt)-2-Chlorotrityl resin is coupled with various amino acids to obtain a protected heptapeptide of formula (2): Boc-D-Phe-Cys(Trt)-Phe-D-Trp-Lys(Boc)-Thr(OBut)-Cys(Trt)-2-Chlorotrityl resin. The linear protected peptide of formula (2) is cleaved from the support using TFA5TIS and water to yield linear protected peptide of formula (3) Boc-D-Phe-Cys(Trt)-Phe-D-Trp-Lys(Boc)-Thr(OBut)-Cys(Trt)-OH Linear protected heptapeptide of formula (3) is deprotected to yield heptapeptide of formula (6): D-Phe-Cys-Phe-D-Tip-Lys-Thr-Cys-OH; which is cyclized using hydrogen peroxide and to the cyclic peptide of formula (7) D-Phe-Cys-Phe-D-Trp-Lys-Thr-Cys-OH; threoninol is coupled at C terminal to yield octreotide.

Abstract: This invention relates a process for preparing octreotide and derivatives thereof. The starting material, Cys(Trt)-2-Chlorotrityl resin is coupled with various amino acids to obtain a protected heptapeptide of formula (2): Boc-D-Phe-Cys(Trt)-Phe-D-Trp-Lys(Boc)-Thr(OBut)-Cys(Trt)-2-Chlorotrityl resin. The linear protected peptide of formula (2) is cleaved from the support using TFA5TIS and water to yield linear protected peptide of formula (3) Boc-D-Phe-Cys(Trt)-Phe-D-Trp-Lys(Boc)-Thr(OBut)-Cys(Trt)-OH Linear protected heptapeptide of formula (3) is deprotected to yield heptapeptide of formula (6): D-Phe-Cys-Phe-D-Tip-Lys-Thr-Cys-OH; which is cyclized using hydrogen peroxide and to the cyclic peptide of formula (7) D-Phe-Cys-Phe-D-Trp-Lys-Thr-Cys-OH; threoninol is coupled at C terminal to yield octreotide.

Abstract: The present invention relates to an improved process for the large scale synthesis of cyclic heptapeptide using Fmoc solid phase synthesis technique. The described process assembles the peptide on a solid support resin by coupling to one another by peptide bonds to obtain a peptide wherein the coupling of cysteine to the resin employs a combination of solvents to reduce cysteine racemization. The process described relates to the use of C1-C4 alcohols as total substitute to organic nitriles thus making the process cost effective, non-toxic and eco-friendly.

Abstract: The present invention relates to an improved process for the preparation of N6-(aminoiminomethyl)-N2-(3-mercapto-1-oxopropyl)-L-lysylglycyl-L-?-aspartyl-L-tryptophyl-L-prolyl-L-cysteinamide, cyclic(1?6)-disulfide of formula (1), which involves assembling a peptide chain comprising of six amino acids and a thioalkyl carboxylic acid in a required sequence on a solid support to obtain a peptide bound resin of formula (2), capping the free amino groups after each coupling, cleaving Dde group in the peptide of formula (2) from the solid support to obtain peptide-solid support of formula (3), guanylating the peptide of formula (3) at ?-lysine-NH2 in an organic solvent to obtain peptide-solid support of formula (4), cleaving and deprotecting all groups in the peptide of formula (4) from the solid support to obtain peptide-amide formula (5), oxidizing the SH-peptide of formula (5) with an appropriate oxidizing agent to obtain the crude peptide-amide of formula (1) and purifying the crude peptide-amide of formula (1)

Abstract: The present invention relates to an improved process for the preparation of N6-(aminoiminomethyl)-N2-(3-mercapto-1-oxopropyl-L-lysylglycyl-L-?-aspartyl-L-tryptophyl-L-prolyl-L-cysteinamide, cyclic(1?6)-disulfide of formula (1), which involves assembling amino acid residues and a thioalkyl carboxylic acid with appropriate protecting groups on a solid phase resin, cleaving the peptide thus obtained from the resin with concomitant removal of side chain protecting groups except Acm protecting group of thiol moiety to obtain peptide amide of formula (3), converting lysine residue of peptide amide of formula (3) having protected thiol group to homoarginine residue by guanylation to obtain peptide of formula (4), preparing silver peptide of formula (5), followed by simultaneous deprotection, obtaining silver peptide of formula (5) and oxidation of silver peptide to obtain crude peptide amide comprising compound of formula (1) and finally subjecting to chromatographic purification.

Abstract: The present invention relates to an improved process for the preparation of N6-(aminoiminomethyl)-N2-(3-mercapto-1-oxopropyl)-L-lysylglycyl-L-?-aspartyl-L-tryptophyl-L-prolyl-L-cysteinamide, cyclic(16)-disulfide of formula (1), which involves assembling a peptide chain comprising of six amino acids and a thioalkyl carboxylic acid in a required sequence on a solid support to obtain a peptide bound resin of formula (2), capping the free amino groups after each coupling, cleaving Dde group in the peptide of formula (2) from the solid support to obtain peptide-solid support of formula (3), guanylating the peptide of formula (3) at ?-lysine-NH2 in an organic solvent to obtain peptide-solid support of formula (4), cleaving and deprotecting all groups in the peptide of formula (4) from the solid support to obtain peptide-amide formula (5), oxidizing the SH-peptide of formula (5) with an appropriate oxidizing agent to obtain the crude peptide-amide of formula (1) and purifying the crude peptide-amide of formula (1) b