1383567-59-6

Basic information

• Product Name: Bis-PEG13-PFP ester
• Synonyms: Bis-PEG13-PFP ester
• CAS NO: 1383567-59-6
• Molecular Formula: C₄₂H₅₆F₁₀O₁₇
• Molecular Weight: 1022.87
• Mol File: 1383567-59-6.mol

Chemical Properties

• Boiling Point: 817.3±65.0 °C(Predicted)
• Appearance: /
• Density: 1.312±0.06 g/cm3(Predicted)
• Solubility: Soluble in DMSO, DCM, DMF
• CAS DataBase Reference: Bis-PEG13-PFP ester(CAS DataBase Reference)
• NIST Chemistry Reference: Bis-PEG13-PFP ester(1383567-59-6)
• EPA Substance Registry System: Bis-PEG13-PFP ester(1383567-59-6)

Safety Data

• Hazardous Substances Data: 1383567-59-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Bis-PEG13-PFP ester is used as a conjugation agent for improving the solubility and stability of therapeutic molecules. The expression is: Bis-PEG13-PFP ester is used as a conjugation agent for [therapeutic molecule] to enhance its solubility and stability in aqueous media.
Used in Drug Delivery Systems:
Bis-PEG13-PFP ester is used as a component in the development of drug delivery systems, particularly for targeted drug delivery. The expression is: Bis-PEG13-PFP ester is used as a component in [drug delivery system] for targeted drug delivery, allowing for the attachment of therapeutic molecules to the delivery vehicle.
Used in Bioconjugation:
Bis-PEG13-PFP ester is used as a bioconjugation agent for the attachment of biologically active molecules, such as peptides, proteins, or nucleic acids, to various surfaces or other molecules. The expression is: Bis-PEG13-PFP ester is used as a bioconjugation agent for [biological molecule] to facilitate its attachment to [target surface or molecule].
Used in Diagnostic Applications:
Bis-PEG13-PFP ester can be used in the development of diagnostic tools, such as imaging agents or biosensors, by attaching specific recognition elements to the PEG linker. The expression is: Bis-PEG13-PFP ester is used as a component in [diagnostic tool] for attaching recognition elements to enable specific detection or imaging.

Upstream product

• 1053656-79-3 4,7,10,13,16,19,22,25,28,31,34,37,40-tridecaoxatritetracontanedioic acid 
• 771-61-9 2,3,4,5,6-pentafluorophenol 

Downstream Products

• 1383567-61-0 PfpOOC-CH₂CH₂O(CH₂CH₂O)12CH₂CH₂-CONHC₄H₉ 

Relevant articles and documents

Modified peptides as potent inhibitors of the PSD-95/NMDA receptor interaction

The present invention is directed to the provision of small molecule inhibitors of the PSD-95/NMDA receptor interaction, employing an undecapeptide corresponding to the C-terminal of the NMDA as a template for finding lead candidates. A compound (NMDAR/PSD-95 inhibitor) of the invention includes a peptide or peptide analogue comprising at least four peptide bonded residues having the sequence YTXV or YSXV, wherein Y is selected from among E, Q, and A, or an analogue thereof and X is selected from among A, Q, D, N, N-Me-A, N-Me-Q, N-Me-D, and N-Me-N or an analogue thereof, wherein an amino-terminal residue of the peptide is N-alkylated. Alternatively the compound of the invention comprises a first peptide or peptide analogue linked to a second peptide or peptide analogue by a linker, where the first and second peptide or peptide analogue each comprise at least four peptide bonded residues having the sequence YTXV or YSXV, wherein Y is selected from among E, Q, and A, or an analogue thereof, and X is selected from among A, Q, D, N, N-Me-A, N-Me-Q, N-Me-D, and N-Me-N or an analogue thereof.

Dimeric analogs of immunosuppressive decapeptide fragment of ubiquitin

Our previous studies revealed that ubiquitin and its decapeptide fragment with the LEDGRTLSDY sequence, located on the exposed molecule loop, strongly suppressed the immune response. This suggested that the loop may serve as a functional epitope of ubiquitin molecule and that a possible mechanism of biological action of the synthesized peptides is associated with interfering in interactions of ubiquitin with other molecules. Ubiquitin is known to exist in oligomeric forms, which can interact with various oligomeric receptors. We designed and synthesized new dimeric analogs of the ubiquitin fragment, to probe whether dimeric peptides may have higher affinity towards the ubiquitin receptors responsible for immunosuppression, which are believed to form oligomeric structures. Three dimerization strategies, N-terminus to N-terminus, C-terminus to C-terminus, and N-terminus to C-terminus (head-to-tail) via PEG derivatives were used to synthesize the dimeric peptides on solid support. In the course of our research, we developed a new and straightforward procedure of dimerization where α-amino groups of the C-terminal lysine residues of two peptide fragments were linked by PEG spacer directly on solid support. The effect of dimeric analogs on the immunological response was tested in the AFC in vitro experiment. The immunological tests showed that the head-to-tail dimerization caused a more profound increase in the biological activity than other tested dimerization methods. Our results suggest that such orientation of peptide components may correspond to orientation of the hypothetic ubiquitin receptors responsible for the immunomodulatory activity.