CXCR4 (N-Terminus) Peptide
- Known as:
- CXCR4 (N-Terminus) Peptide
- Catalog number:
- 1009P
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- CXCR4 (N-Terminus) Peptide
Related genes to: CXCR4 (N-Terminus) Peptide
- Gene:
- CXCR4 NIH gene
- Name:
- C-X-C motif chemokine receptor 4
- Previous symbol:
- -
- Synonyms:
- LESTR, NPY3R, HM89, NPYY3R, D2S201E, fusin, HSY3RR, NPYR, CD184
- Chromosome:
- 2q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-17
- Date modifiied:
- 2019-04-23
Related products to: CXCR4 (N-Terminus) Peptide
Related articles to: CXCR4 (N-Terminus) Peptide
- The clustering states of cell surface C-X-C chemokine receptor 4 (CXCR4) play a critical role in cancer metastasis. We previously reported a "Pro-Clustering Polymers (PCP)" system, P-BS-CM1 → P-CM2, for the treatment of metastatic triple-negative breast cancer (TNBC). Subsequent studies demonstrated that PCP enhanced CXCR4 blockade and metastasis suppression by disrupting CXCR4 association-disassociation dynamic equilibrium and shifting the receptor toward a hyper-clustered state. As an alternative strategy to disrupt this equilibrium, shifting CXCR4 toward a less clustered, more dispersed state, i.e., inhibiting CXCR4 clustering, remains largely underexplored. Herein, we developed a "De-Clustering Polymer (DCP)" system, P-BS-pHLIP, which introduces steric hindrance to block receptor-receptor interactions and thereby inhibits CXCR4 clustering. Side-by-side comparisons of DCP with our previously developed PCP system revealed that different modes of CXCR4 manipulation dictate divergent downstream biological outcomes. PCP preferentially impaired tumor cell motility by inducing mitochondrial dysfunction and energy depletion, whereas DCP preferentially reduced tumor cell adhesiveness by downregulating multiple adhesion molecules. Both PCP and DCP exert potent anti-metastatic efficacy in multiple TNBC metastatic models. Collectively, this study demonstrates that engineered polymeric systems that biophysically manipulate receptor clustering states, via either pro-clustering or de-clustering, represent promising therapeutic strategies for suppressing cancer metastasis. - Source: PubMed
Publication date: 2026/09/20
Liu ChendongShi JunzhuShi LikaiJia QingruiLiu JiaqiYan YueZhou MingluZhou ZhouHuang YuanLi Lian - Migration of lung cancer cells to distant sites is largely mediated by the CXCR4/CXCL12 axis. Meanwhile, 1,2,4-triazole derivatives have shown antiproliferative activity in lung cancer and have been reported to inhibit metastasis in pancreatic and breast cancer. - Source: PubMed
Publication date: 2026/08/18
Yeni YeniKurniawan FransiskaPermana BennyTjahjono Daryono Hadi - Surface plasmon resonance (SPR) biosensor has emerged as a transformative tool in high-throughput drug screening and label-free analysis of biomolecular interactions. However, a critical limitation of SPR lies in its stringent requirement for highly purified proteins to ensure reliable quantification of binding affinities and kinetic parameters. In order to address the limitations, the lentiviral particle (LVP) and styrene-maleic acid (SMA) polymer have been previously developed to extract and stabilize transmembrane proteins (TMs) indirectly and thus to detect ligands interaction with TMs by SPR biosensor. The present study proposes a high-throughput SPR-based drug screening system that utilizes cell-free protein synthesis (CFPS) to achieve purification and immobilization of TMs on SPR biosensors. First, C-X-C chemokine receptor 4 (CXCR4) protein with histidine (His)-tag was prepared by CFPS. Then, two types of nickel-nitrilotriacetic acid (Ni-NTA) biosensors, modified with carboxymethylated dextran (CMD) and coated with polycarboxylate hydrogel coating (HC) matrix, were compared with classical carboxymethylated dextran 5 (CM5) biosensor in order to determine the optimal strategy for coupling the CXCR4-CFPS protein. The CMD-NTA/SPR biosensor was next applied to screen for CXCR4 ligands from 96 natural products. Finally, glycyrrhizic acid and ginsenoside Re were proved to be function as CXCR4 inhibitors by affinity test, molecular docking, and cell migration assay. The combination of CFPS with SPR technologies facilitates purification and immobilization of target proteins in a single step, thereby significantly enhancing the efficiency of SPR assay procedures. The system has broad applicability for targeting various challenging TMs and provides potential candidates for subsequent drug development. - Source: PubMed
Publication date: 2026/03/24
Wang XiaofeiWang YantingChen HaoXia NingqiGu JiayuZhang LinfengWang DongyaoLu BinLv DiyaChen XiaofeiCao YanChai Yifeng - Radiotheranostic agents enable paired diagnostic imaging and targeted radiopharmaceutical therapy through the selection of appropriate radioisotopes. Radiotheranostics are typically composed of a targeting vector, a chelator or prosthetic group for radiolabeling and an optional linker for optimizing their pharmacokinetic properties. The chemokine receptor 4 (CXCR4) is a promising target for molecular imaging and therapy across a broad range of pathological conditions, including cancer, cardiovascular disorders, infectious and autoimmune diseases. The elucidation of CXCR4 crystal structures, together with extensive structure-activity relationship studies, has accelerated the design of novel small molecule and peptide-based CXCR4-targeted radiopharmaceuticals. These molecules have served as scaffolds that can be chemically modified to optimize their pharmacokinetic properties and maximize accumulation at the target organ. In oncology, the peptide-based theranostic pair Pentixafor/Pentixather has advanced into early-stage clinical evaluations for imaging and therapy. This review summarizes the current landscape of CXCR4 radiopharmaceuticals, and highlights key structural features and chemical modifications that lead to enhanced receptor affinity as well as improved pharmacokinetic and targeting properties for theranostic applications. - Source: PubMed
Publication date: 2026/09/04
Astiazarán-Rascón Itzel ReneéLau JosephBénard François - - Source: PubMed
Publication date: 2026/09/19
El-Shoura Ehab A MMohamed Ahmed A NAtwa Ahmed MSalem Esraa ASharkawi Souty M ZSelim Hend MostafaElberri Aya IbrahimGawesh El-SayedAhmed Yasmine HAbd El-Ghafar Omnia A M