13198-06-6

Usage

InChI:InChI=1/C46H69N11O10S/c1-27(2)22-34(44(65)53-31(40(49)61)18-21-68-3)52-39(60)26-51-41(62)35(24-29-14-16-30(58)17-15-29)55-45(66)36(23-28-10-5-4-6-11-28)56-43(64)33(12-7-8-19-47)54-46(67)37(25-38(48)59)57-42(63)32-13-9-20-50-32/h4-6,10-11,14-17,27,31-37,50,58H,7-9,12-13,18-26,47H2,1-3H3,(H2,48,59)(H2,49,61)(H,51,62)(H,52,60)(H,53,65)(H,54,67)(H,55,66)(H,56,64)(H,57,63)/t31?,32-,33-,34-,35-,36-,37-/m0/s1

Upstream product

• 4530-20-5 BOC-glycine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 2488-15-5 N-tert-butoxycarbonyl-L-methionine 
• 75974-78-6 Boc-Tyr(Br-Z)-OH 

Relevant academic research and scientific papers

Bond cleavage reactions in solid aqueous carbohydrate solutions

Purpose. To investigate chemical reactivity in water soluble glasses. Methods. Rates of bond cleavage reactions in freeze-dried and freeze- concentrated aqueous carbohydrate solutions were measured above and below the glass transition temperatures (T(g)). The kinetics of two reactions have been determined in formulations containing di- and polysaccharides: (1) fission of the Asp-Pro peptide bond in Physalaemin and Hamburger peptide by following the release of proline, using a ninhydrin based reaction and (2) the unimolecular dissociation of 2(4-nitrophenoxy) tetrahydropyran by following the release of the 4-nitrophenoxy anion. Results. The results show clearly that reaction occurs below the glass transition temperature, albeit at very reduced rates. No significant enhancement of the temperature dependence of the rate constant was observed near T(g). Different water soluble glasses provide different degrees of stability. The order of stabilisation was sucrose>Ficoll (low mol. weight)>Byco A ? Ficoll (high mol. weight)>dextran. The density of the matrix, and therefore the degrees of freedom of mobility of the reactant, is thought to be responsible for these differences. Conclusions. The storage of therapeutic agents, such as proteins, in glassy matrices below T(g) does not confer indefinite stability. When formulating products, notice should be taken of the differing stabilisation properties of excipients.

Hydrolytic cleavage of pyroglutamyl-peptide Bond. V. Selective removal of pyroglutamic acid from biologically active pyroglutamylpeptides in high concentrations of aqueous methanesulfonic acid

Application of aqueous methanesulfonic acid (MSA) for selective chemical removal of pyroglutamic acid (pGlu) residue from five biologically active pyroglutamyl-peptides (pGlu-X-peptides, X=amino acid residue at position 2) was examined. Gonadotropin releasing hormone (Gn-RH), dog neuromedin U-8 (d-NMU-8), physalaemin (PH), a bradykinin potentiating peptide (BPP-5a) and neurotensin (NT) as pGlu-X-peptides were incubated in either 70% or 90% aqueous MSA at 25°C. HPLC analysis of the incubation solutions showed that the main decomposition product was H-X-peptide derived from each pGlu-X-peptide by the removal of pGlu. The results revealed that the pGlu-X peptide bond had higher susceptibility than various internal amide bonds in the five peptides examined, including the Trp-Ser bond in Gn-RH, the C-terminal Asn-NH2 in d-NMU-8, and the Asp-Pro bond in PH, whose acid susceptibility is well known. Thus, mild hydrolysis with high concentrations of aqueous MSA may be applicable to chemically selective removal of pGlu from pGlu-X-peptides for structural examinations.