139592-37-3

Usage

Uses

Used in Pharmaceutical Research:
(FMOC-CYS-OTBU)2, (DISULFIDE BOND) is used as a building block for the synthesis of peptides and proteins with specific properties. The disulfide bond in (FMOC-CYS-OTBU)2, (DISULFIDE BOND) is crucial for the stability and biological activity of the resulting molecules, making it an essential component in the development of new drugs and therapeutic agents.
Used in Chemical Synthesis:
In the field of chemical synthesis, (FMOC-CYS-OTBU)2, (DISULFIDE BOND) serves as a versatile intermediate for the preparation of various complex organic molecules. Its unique structure allows for the formation of a wide range of compounds with diverse applications, including pharmaceuticals, agrochemicals, and materials science.
Used in Material Science:
(FMOC-CYS-OTBU)2, (DISULFIDE BOND) is used as a component in the development of novel materials with specific properties, such as improved mechanical strength, thermal stability, or chemical resistance. The disulfide bond in (FMOC-CYS-OTBU)2, (DISULFIDE BOND) can be exploited to create materials with tailored characteristics, making it a valuable asset in the field of material science.
Used in Biotechnology:
In biotechnology, (FMOC-CYS-OTBU)2, (DISULFIDE BOND) is used as a key component in the design and synthesis of bioactive peptides and proteins. The disulfide bond can be employed to introduce specific structural features or to stabilize the bioactive conformation of these molecules, which can be crucial for their biological activity and potential applications in medicine and agriculture.
Overall, (FMOC-CYS-OTBU)2, (DISULFIDE BOND) is a versatile and valuable research chemical with a wide range of applications in various industries, including pharmaceuticals, chemical synthesis, material science, and biotechnology. Its unique structure and properties make it an essential tool for the development of new drugs, materials, and technologies.

Physical Form

Solid

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 62574-13-4 L-cystine tert-butyl ester 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 540-88-5 acetic acid tert-butyl ester 
• 56-89-3 L-cystine 
• 98946-18-0 tert-Butyl 2,2,2-trichloroacetimidate 
• 135273-01-7 N,N'-bis[(9H-fluoren-9-ylmethoxy)carbonyl]-L-cystine 

Downstream Products

• 1337527-20-4 (R)-3-((R)-2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-3-(4-(3-(diethoxyphosphoryl)propoxy)phenethylamino)-3-oxopropylthio)propane-1,2-diyl didodecanoate 
• 1337527-22-6 (R)-3-((R)-2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-3-(6-(benzyloxy)-6-oxohexylamino )-3-oxopropylthio)propane-1,2-diyl didodecanoate 
• 1337526-95-0 (4R,7S,10R,14R)-benzyl 10-(((9H-fluoren-9-yl)methoxy)carbonylamino)-4-carbamoyl-7-ethyl-14-(hexadecyloxy)-6,9-dioxo-16-oxa-12-thia-5,8-diazadotriacontan-1-oate 
• 139573-77-6 N-(((9H-fluoren-9-yl)methoxy)carbonyl)-S-((R)-2,3-bis(palmitoyloxy)propyl)-L-cysteine 
• 191993-89-2 (R)-3-[(R)-2-tert-Butoxycarbonyl-2-(9H-fluoren-9-ylmethoxycarbonylamino)-ethylsulfanyl]-2-(trityl-amino)-propionic acid benzyl ester 
• 67413-25-6 benzyl (-)-(2S)-1-trityl-aziridine-2-carboxylate 
• 503565-02-4 (2S,6R)-N²-triphenylmethyl-N⁶-(9H-fluorenylmethoxycarbonyl)-lanthionine O¹-allyl-O⁷-tert-butyl ester 

Relevant academic research and scientific papers

Solid-supported synthesis and biological evaluation of the lantibiotic peptide bis(desmethyl) lacticin 3147 A2

(Chemical Equation Presented) Lan-tastic! A lanthionine analogue of lacticin 3147 A2 (Lan-A2, 2) containing multiple thioether bridges (see picture) has been successfully synthesized by a combination of solid- and solution-phase peptide synthesis. Chemically synthesized Lan-A2 (2) exhibits synergistic biological activity similar to natural lacticin A2 (1) in the presence of natural lacticin A1 against Gram-positive bacteria.

Design and Evolution of a Macrocyclic Peptide Inhibitor of the Sonic Hedgehog/Patched Interaction

The hedgehog (Hh) signaling pathway plays a central role during embryonic development, and its aberrant activation has been implicated in the development and progression of several human cancers. Major efforts toward the identification of chemical modulators of the hedgehog pathway have yielded several antagonists of the GPCR-like smoothened receptor. In contrast, potent inhibitors of the sonic hedgehog/patched interaction, the most upstream event in ligand-induced activation of this signaling pathway, have been elusive. To address this gap, a genetically encoded cyclic peptide was designed based on the sonic hedgehog (Shh)-binding loop of hedgehog-interacting protein (HHIP) and subjected to multiple rounds of affinity maturation through the screening of macrocyclic peptide libraries produced in E. coli cells. Using this approach, an optimized macrocyclic peptide inhibitor (HL2-m5) was obtained that binds Shh with a KD of 170 nM, which corresponds to a 120-fold affinity improvement compared to the parent molecule. Importantly, HL2-m5 is able to effectively suppress Shh-mediated hedgehog signaling and Gli-controlled gene transcription in living cells (IC50 = 230 nM), providing the most potent inhibitor of the sonic hedgehog/patched interaction reported to date. This first-in-class macrocyclic peptide modulator of the hedgehog pathway is expected to provide a valuable probe for investigating and targeting ligand-dependent hedgehog pathway activation in cancer and other pathologies. This work also introduces a general strategy for the development of cyclopeptide inhibitors of protein-protein interactions.

Diaminodiacid bridge improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A

The replacement of the disulfide bridge of CPI-1, a peptide inhibitor of light chain of Botulinum toxin serotype A, with the thioether-containing and biscarba-containing diaminodiacid bridge leads to a significant decrease in the degradation by trypsin and increase in the detoxification activity in vivo, the addition of hydrophobic or positive amino acid at C-terminus of modified peptides further improves the inhibitory activity.

Synthesis and Evaluation of Novel TLR2 Agonists as Potential Adjuvants for Cancer Vaccines

Cancer immunotherapy has gained increasing attention due to its potential specificity and lack of adverse side effects when compared to more traditional modes of treatment. Toll-like receptor 2 (TLR2) agonists are lipopeptides possessing the S-[2,3-bis(palmitoyloxy)propyl]-l-cysteine (Pam2Cys) motif and exhibit potent immunostimulatory effects. These agonists offer a means of providing "danger signals" in order to activate the immune system toward tumor antigens. Thus, the development of TLR2 agonists is attractive in the search of potential immunostimulants for cancer. Existing SAR studies of Pam2Cys with TLR2 indicate that the structural requirements for activity are, for the most part, very intolerable. We have investigated the importance of stereochemistry, the effect of N-terminal acylation, and homologation between the two ester functionalities in Pam2Cys-conjugated lipopeptides on TLR2 activity. The R diastereomer is significantly more potent than the S diastereomer and N-terminal modification generally lowers TLR2 activity. Most notably, homologation gives rise to analogues which are comparatively active to the native Pam2Cys containing constructs.

Synthesis of Peptide Disulfide-Bond Mimics by Using Fully Orthogonally Protected Diaminodiacids

A new strategy was developed for the synthesis of peptide disulfide-bond mimics using fully orthogonally protected diaminodiacids. This method overcomes the previous problems of heavy-metal contamination and poor compatibility with Fmoc chemistry and provides a practical avenue for the efficient preparation of peptide disulfide-bond mimics.

CYCLIC PEPTIDE INHIBITORS OF HEDGEHOG PROTEINS

Cyclic peptide compounds are provided that can bind to one or more homologs of Hedghehog signaling proteins and block their interaction with the Patched receptor. These compounds are useful for suppressing Hedgehog-dependent stimulation of the Hedgehog pathway in cells and in living organisms. Methods for using the cyclic peptide compounds, and compositions comprising them, for treatment of cancers and other diseases which are characterized by aberrant Hedgehog-dependent activation of the Hedgehog pathway and/or which can benefit from chemical suppression of Hedgehog-dependent signaling are also disclosed.

Synthesis and Bioactivity of Diastereomers of the Virulence Lanthipeptide Cytolysin

Cytolysin, a two-component lanthipeptide comprising cytolysin S (CylLS″) and cytolysin L (CylLL″), is the only family member to exhibit lytic activity against mammalian cells in addition to synergistic antimicrobial activity. A subset of the thioether cross-links of CylLS″ and CylLL″ have ll stereochemistry instead of the canonical dl stereochemistry in all previously characterized lanthipeptides. The synthesis of a CylLS″ variant with dl stereochemistry is reported. Its antimicrobial activity was found to be decreased, but not its lytic activity against red blood cells. Hence, the unusual ll stereochemistry is not responsible for the lytic activity.

Diaminodiacid-based solid-phase synthesis of peptide disulfide bond mimics

The antimicrobial peptide tachyplesin I was used as a model to apply the title strategy, which was developed for the preparation of peptidic macrocycles with double disulfide surrogates. The folding and activity of the tachyplesin I analogues were found to be sensitive to the structure of the disulfide surrogates, thus underlining the necessity of a flexible synthetic route for generating disulfide bond surrogates with high structural diversity. Copyright

Chemical synthesis and biological activity of analogues of the lantibiotic epilancin 15X

Lantibiotics are a large family of antibacterial peptide natural products containing multiple post-translational modifications, including the thioether structures lanthionine and methyllanthionine. Efforts to probe structure-activity relationships and engineer improved pharmacological properties have driven the development of new methods to produce non-natural analogues of these compounds. In this study, solid-supported chemical synthesis was used to produce analogues of the potent lantibiotic epilancin 15X, in order to assess the importance of several N-terminal post-translational modifications for biological activity. Surprisingly, substitution of these moieties, including the unusual N-terminal d-lactyl moiety, resulted in relatively small changes in the antimicrobial activity and pore-forming ability of the peptides.

Synthesis and activity of thioether-containing analogues of the complement inhibitor compstatin

Disulfide bonds are essential for the structural stability and biological activity of many bioactive peptides. However, these bonds are labile to reducing agents, which can limit the therapeutic utility of such peptides. Substitution of a disulfide bond w