91037-75-1

Usage

Uses

Used in Biomedical Research:
GRGDSP is utilized as a research tool for studying the role of integrins in cell adhesion and signaling, providing insights into cell behavior and interactions with the extracellular matrix.
Used in Tissue Engineering:
GRGDSP is employed as a bioactive component in tissue engineering, where it serves to enhance cell adhesion, migration, and proliferation, thereby promoting tissue regeneration and repair.
Used in Drug Delivery Systems:
In the pharmaceutical industry, GRGDSP can be used as a targeting moiety for drug delivery systems, specifically for the development of integrin-targeted therapies, to improve the specificity and efficacy of drug delivery to cells expressing integrins.
Used in Regenerative Medicine:
GRGDSP is applied as a component in regenerative medicine to stimulate the formation of new blood vessels and support tissue regeneration, which is crucial for the healing process and restoration of damaged tissues.
Used in Diagnostics:
GRGDSP can be utilized in diagnostic assays to assess the presence and activity of integrins, which can be indicative of certain disease states or responses to therapeutic interventions.

InChI:InChI=1/C22H37N9O10/c23-8-15(33)28-11(3-1-5-26-22(24)25)18(37)27-9-16(34)29-12(7-17(35)36)19(38)30-13(10-32)20(39)31-6-2-4-14(31)21(40)41/h11-14,32H,1-10,23H2,(H,27,37)(H,28,33)(H,29,34)(H,30,38)(H,35,36)(H,40,41)(H4,24,25,26)/t11-,12-,13+,14-/m0/s1

Upstream product

• 23680-31-1 BOC-O-benzyl-L-serine 
• 73821-95-1 Boc-Asp(O-cyclohexyl)-OH 
• 207857-15-6 1,3-di(tert-butyloxycarbonyl)-2-(trifluoromethylsulfonyl)guanidine 
• 150828-96-9 Boc-Orn(Fmoc)-OH 

Relevant academic research and scientific papers

Fibrinogen-coated particles for therapeutic use

The invention provides a particle comprising fibrinogen bound on the surface of an albumin matrix, wherein said particle is capable of coaggregation with platelet, and of aggregation in a solution containing soluble fibrinogen at a concentration of soluble fibrinogen not capable by it self of formation of a clot upon activation by thrombin.

Triurethane-protected guanidines and triflyldiurethane-protected guanidines: New reagents for guanidinylation reactions

New guanidinylation reagents are reported. These reagents consist of N,N',N''-tri-Boc-guanidine (1) and N,N',N''-tri-Cbz-guanidine (2), which allow for the facile conversion of alcohols to substituted guanidines. A series of arginine analogues were synthesized via condensation of a primary or secondary alcohol with the guanidinylation reagents 1 or 2, under Mitsunobu conditions, to produce protected alkylated guanidines. In addition, an extended study of the previously reported reagents N,N'-di-Boc-N''- triflylguanidine (3) and N,N'-di-Cbz-N''-triflylguanidine (4) is presented. The triflyldiurethane-protected guanidine 3 was utilized to guanidinylate primary and secondary amines under mild conditions with high yield in both solution and on solid phase.

Non-crosslinked protein particles for therapeutic and diagnostic use

Albumin particles in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolubilization without the aid of a crosslinking agent and without denaturation, by the incorporation of a stabilizing agent in the particle composition. Particles which are primarily albumin in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolublization by the incorporation of a reducing agent, oxidizing agent, hydrogen-accepting molecule, high molecular weight polymer, sulfur-containing ring compound or combinations thereof.

Non-crosslinked protein particles for therapeutic and diagnostic use

Albumin particles in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolubilization without the aid of a crosslinking agent and without denaturation, by the incorporation of hemoglobin in the particle composition. Particles which are primarily hemoglobin in the nanometer and micrometer size range in an aqueous suspension are rendered stable against aggregation by the incorporation of either albumin, surface active agents or gelatin.