61950-59-2

Usage

Uses

Used in Medical Applications:
(D-TRP8,D-CYS14)-SOMATOSTATIN-14 is used as a therapeutic agent for the treatment of various conditions, including acromegaly, neuroendocrine tumors, and gastrointestinal disorders. Its ability to inhibit the release of hormones such as insulin, glucagon, growth hormone, and other gastrointestinal hormones makes it a valuable tool in managing these conditions.
Used in Research:
In the scientific community, (D-TRP8,D-CYS14)-SOMATOSTATIN-14 is used as a research tool to study the effects of somatostatin and its role in the endocrine system. Its synthetic nature allows for controlled experiments and a better understanding of hormone regulation and related physiological processes.
Used in Pharmaceutical Development:
(D-TRP8,D-CYS14)-SOMATOSTATIN-14 is utilized in the development of pharmaceuticals targeting endocrine-related conditions. Its potential in treating acromegaly, neuroendocrine tumors, and gastrointestinal disorders has led to its incorporation in the formulation of drugs aimed at managing these health issues.
Used in Diagnostic Applications:
In the field of diagnostics, (D-TRP8,D-CYS14)-SOMATOSTATIN-14 serves as a marker for the detection and monitoring of endocrine disorders. Its interaction with various hormones can help in identifying imbalances and providing insights into the underlying causes of certain conditions.
Used in Application Industry:
(D-TRP8,D-CYS14)-SOMATOSTATIN-14 is used as a regulatory agent in the pharmaceutical industry for the development of drugs targeting endocrine disorders, providing a means to control hormone release and manage related health conditions effectively.

InChI:InChI=1/C76H104N18O19S2/c1-41(79)64(100)82-37-61(99)83-58-39-114-115-40-59(76(112)113)92-72(108)57(38-95)91-75(111)63(43(3)97)94-71(107)54(33-46-23-11-6-12-24-46)90-74(110)62(42(2)96)93-66(102)51(28-16-18-30-78)84-69(105)55(34-47-36-81-49-26-14-13-25-48(47)49)88-68(104)53(32-45-21-9-5-10-22-45)86-67(103)52(31-44-19-7-4-8-20-44)87-70(106)56(35-60(80)98)89-65(101)50(85-73(58)109)27-15-17-29-77/h4-14,19-26,36,41-43,50-59,62-63,81,95-97H,15-18,27-35,37-40,77-79H2,1-3H3,(H2,80,98)(H,82,100)(H,83,99)(H,84,105)(H,85,109)(H,86,103)(H,87,106)(H,88,104)(H,89,101)(H,90,110)(H,91,111)(H,92,108)(H,93,102)(H,94,107)(H,112,113)/t41-,42+,43+,50-,51-,52-,53-,54-,55+,56-,57-,58-,59+,62?,63?/m0/s1

Upstream product

• 27025-41-8 Oxidized glutathione 
• 40958-31-4 Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys 
• 4530-20-5 BOC-glycine 
• 15761-38-3 L-N-Boc-Ala 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 15260-10-3 N-Boc-O-benzyl-L-threonine 
• 23680-31-1 BOC-O-benzyl-L-serine 
• 18942-46-6 N-(tert-butyloxycarbonyl)-S-(4-methoxybenzyl)cysteine 
• 54613-99-9 Boc-(S)-Lys(2-Cl-Z)-OH 
• 13139-14-5 Boc-Trp-OH 
• 65420-40-8 (S)-2-tert-Butoxycarbonylamino-N-(9H-xanthen-9-yl)-succinamic acid 
• 5241-64-5 Boc-D-Trp-OH 
• 1324007-69-3 C₁₇₈H₂₆₈N₁₈O₂₉S₂ 

Downstream Products

• 1266665-23-9 C₈₄H₁₁₄N₂₀O₂₁S₂ 

Relevant academic research and scientific papers

Formation of peptide disulfide bonds through a trans-dibromido-Pt(IV) complex oxidation reaction: Kinetic and mechanistic analyses

A trans-dibromido-Pt(IV) complex [PtBr2(en)2]Br2 was synthesized and evaluated for the synthesis of peptide disulfide bonds in this work. The reactions between the Pt(IV) complex and dicysteine-containing peptides were carried out in various aqueous solutions. As a result, excellent yields with fast reaction rates were achieved. Methionine residue was intact when the Pt(IV) complex reacted with a dicysteine and methionine-containing peptide. 3,6-Dioxa-1,8-octanedithiol (DODT) was selected as a model compound of the dicysteine-containing peptide. Kinetic studies for the reaction between the Pt(IV) complex and DODT were performed in different pH solutions. It is first-order both in [Pt(IV)] and in [DODT]. A reaction mechanism was proposed accordingly. The kinetic and mechanistic results demonstrated that the reaction rate for the formation of peptide disulfide bond via the Pt(IV) oxidation is increased with the increase of pH of the reaction medium. The protolytic constants of the two thiol groups in peptide also play a critical role in reaction rate. On the other hand, kinetic studies demonstrated that the Pt(IV) complex trans-[PtBr2(en)2]2+ can be used in an acidic medium for the purpose of synthesis of disulfide bonds.

Construction of disulfide bonds in peptides via immobilized platinum(IV) complex oxidation

A novel TentaGel resin supported platinum(IV) complex named TentaGel-Pt(IV) was synthesized and characterized by SEM, XPS, ICP-MS and UV–vis spectrophotometry. The formation of intramolecular disulfides in eleven dithiol-containing peptides of variable lengths using TentaGel-Pt(IV) was investigated at room temperature. The disulfide-containing peptides were formed in excellent oxidation yields and were easily separated by filtration upon completion of the reaction. Excellent reusability of TentaGel-Pt(IV) was also achieved. The mechanism for construction of the disulfide bond in peptides via TentaGel-Pt(IV) oxidation was proposed.

A study to develop platinum(iv) complex chemistry for peptide disulfide bond formation

Platinum(iv) complexes with a heterocyclic ligand and an ancillary ligand have been investigated and applied for treating various tumour cell lines. Another application of the Pt(iv) complexes in forming peptide disulfide bonds was investigated in this work. For development of Pt(iv) complex chemistry for disulfide bond formation in peptides, two Pt(iv) complexes, [PtCl2(phen)(en)]Cl2 and [PtCl2(bpy)(en)]Cl2, were synthesized and characterized using elemental analysis, ESI-MS and NMR. Subsequently, they were investigated as oxidants for the formation of disulfide bonds in various peptides. Excellent purities and yields of disulfide-containing peptides were achieved when the reactions were carried out in aqueous solution. The reactions were completed rapidly in a wide range of pH values even in acidic medium at room temperature. An intramolecular disulfide bond was formed in each of the peptides in a solution containing two dithiol-containing peptides, making the Pt(iv) complexes useful for generating disulfide-containing peptide libraries. In addition, the two Pt(iv) complexes can be used as oxidants for the synthesis of disulfide bonds on a resin, which is a more convenient method to synthesize disulfide-containing peptides through automation.

Robust synthesis of C-terminal cysteine-containing peptide acids through a peptide hydrazide-based strategy

A new robust strategy was reported for the epimerization-free synthesis of C-terminal Cys-containing peptide acids through mercaptoethanol-mediated hydrolysis of peptide thioesters prepared in situ from peptide hydrazides. This simple-to-operate and highly efficient method avoids the use of derivatization reagents for resin modification, thus providing a practical avenue for the preparation of C-terminal Cys-containing peptide acids.

Fine-tuning the π-π Aromatic interactions in peptides: Somatostatin analogues containing mesityl alanine

Going through the motions: Somatostatin analogues having greater conformational rigidity than somatostatin have been prepared by substituting Phe residues in the native sequence with mesityl alanine (Msa; see structure). The analogues show high affinity f

Soluble-support-assisted electrochemical reactions: Application to anodic disulfide bond formation

A soluble-support-assisted technique was successfully applied to electrochemical reactions, leading to anodic disulfide bond formation. The support-bound peptide was soluble in electrolyte solution, allowing electron transfer at the surface of the electrodes. After completion of the reaction, the support-bound product was recovered as a precipitate by simple dilution of the reaction mixture with poor solvent.

N-Imidazolebenzyl-histidine substitution in somatostatin and in its octapeptide analogue modulates receptor selectivity and function

Despite 3 decades of focused chemical, biological, structural, and clinical developments, unusual properties of somatostatin (SRIF, 1) analogues are still being uncovered. Here we report the unexpected functional properties of 1 and the octapeptide cyclo(3-14)H-Cys-Phe-Phe-Trp8-Lys-Thr-Phe-Cys-OH (somatostatin numbering; OLT-8, 9) substituted by imBzl-l- or -d-His at position 8. These analogues were tested for their binding affinity to the five human somatostatin receptors (sst1-5), as well as for their functional properties (or functionalities) in an sst3 internalization assay and in an sst3 luciferase reporter gene assay. While substitution of Trp8 in somatostatin by imBzl-l- or -d-His8 results in sst3 selectivity, substitution of Trp8 in the octapeptide 9 by imBzl-l- or -d-His8 results in loss of binding affinity for sst1,2,4,5 and a radical functional switch from agonist to antagonist.

Pharmaceutical compositions containing growth-hormone inhibitors or their biologically active fragments for the treatment of uterine myomas

Pharmaceutical compositions containing growth-hormone inhibitors or their biologically active fragments for the treatment of uterine myomas are described.

Trans-Dichlorotetracyanoplatinate(IV) as a Reagent for the Rapid and Quantitative Formation of Intramolecular Disulfide Bonds in Peptides

Oxidation of cysteine thiol groups by trans-dichlorotetracyanoplatinate(IV) to form intramolecular peptide disulfide bonds has been studied for a series of dithiol peptides ranging from 4 to 15 amino acid residues in length. The dithiol peptides are rapidly and quantitatively transformed to their intramolecular disulfide forms by a slight excess of [Pt(CN)4Cl2]2-, as shown by HPLC. Quantitative analyses by HPLC and by spectrophotometric titration confirm a [Pt(IV)]:[dithiol peptide] stoichiometry of 1:1. Under the low pH conditions used, oxidation to form a 38-membered ring in the case of reduced somatostatin is as rapid as that to form much smaller rings, suggesting that ring closure is not the rate-determining step. The oxidation rates increase as the pH is increased. Time-resolved spectra show two isosbestic points, indicating that no peptide-platinum intermediates accumulate to a significant amount. A reaction mechanism similar to that for reduction of [Pt(CN)4Cl2]2- by monothiols is proposed. [Pt(CN)4Cl2]2- is a mild oxidant and essentially substitution inert; its reduction product, [Pt(CN)4Cl2]2-, is stable, has no redox chemistry with peptides, and does not form complexes with peptides. Moreover, [Pt(CN)4Cl2]2- and [Pt(CN)4Cl2]2- are nontoxic and readily separable from peptides by HPLC, and the cost of the Pt(IV) complex is negligible compared with that of peptides. The only unwanted side reaction observed with [Pt(CN)4Cl2]2- is oxidation of the sulfur of methionine to the sulfoxide form. These characteristics and the results of this study suggest that [Pt(CN)4Cl2]2- is an excellent reagent for the formation of intramolecular peptide disulfide bonds.

Targeted cytotoxic anthracycline analogs

This invention is in the field of the chemistry of targeting anticancer anthracycline derivatives. More particularly, it concerns doxorubicin (DOX) or its daunosamine modified derivatives (DM-DOX) linked covalently to analogs of peptide hormones such as LH-RH, bombesin and somatostatin. These covalent conjugates are targeted to various tumors bearing receptors for the peptide hormone analogs. The compounds of this invention are represented by General Formula Q14 --O--R--P wherein Q has the general formula STR1 wherein: Q14 signifies a Q moiety with a side chain at the 14 position, R-- is H or --C(O)--(CH2)n --C(O)-- and n=0-7, R' is NH2 or an aromatic, saturated or partially saturated 5 or 6 membered heterocyclic compounds having at least one ring nitrogen and optionally having a butadiene moiety bonded to adjacent carbon atoms of said ring to form a bicyclic system; P is H or a peptide moiety, suitably an LHRH, somatostatin or bombesin analogs. Nevertheless where R' is NH2 then R and P are other than H. When R and P are H, then R' is other than NH2. A novel synthetic reaction has been discovered in the course of this work to form partially saturated heterocyclic moieties from vicinal and disjunct i.e., α, β, or α, γ hydroxy primary amines.