VEGFR Inhibitors

기타 Protein Tyrosine Kinase 억제제

아이소폼 선택적 제품

• 주요 억제제
• 억제제 (105)
• 화학 물질들 (2)

Cat.No.	제품명	정보	제품 사용 인용	제품 검증
S2842	SAR131675	SAR131675는 VEGFR3 억제제로, 무세포 분석(cell-free assays)에서 23 nM/12 nM의 IC50/Ki 값을 가지며, VEGFR1/2 대비 VEGFR3에 대해 약 50배 및 10배 더 높은 선택성을 보이고, Akt1, CDKs, PLK1, EGFR, IGF-1R, c-Met, Flt2 등에 대해서는 거의 활성을 나타내지 않습니다.	Cell Death Discov, 2025, 11(1):320 Zool Res, 2025, 46(6):1317-1325 Cell Signal, 2025, 130:111675
S1010	BIBF 1120 (Nintedanib)	Nintedanib은 VEGFR1/2/3, FGFR1/2/3 및 PDGFRα/β에 대한 강력한 삼중 혈관키나아제(angiokinase) 억제제로, 무세포 분석(cell-free assays)에서 IC50은 각각 34 nM/13 nM/13 nM, 69 nM/37 nM/108 nM 및 59 nM/65 nM입니다. 임상 3상.	Cancer Biology & Medicine, November 19, 2025, 20250275 Thorax, February 18, 2026, thorax-2025-223325 Drug Design, Development and Therapy, February 18, 2022, 397-411
S1119	Cabozantinib (XL184)	0.035 nM의 IC50을 가진 강력한 VEGFR2 억제제인 Cabozantinib (XL184)은 또한 세포 무함유 분석에서 각각 1.3 nM, 4 nM, 4.6 nM, 12 nM/11.3 nM/6 nM, 14.3 nM 및 7 nM의 IC50으로 c-Met, Ret, Kit, Flt-1/3/4, Tie2 및 AXL을 억제합니다. 이는 AKT/GSK-3β/NF-κB 신호 전달 경로를 통해 결장암 세포에서 PUMA 의존성 apoptosis를 유도합니다.	Cell Reports Medicine, September 20, 2022, 100659 Redox Biology, October 21, 2023, 102945 Hepatology Communications, November 8, 2023, e0313
S1164	E7080 (Lenvatinib)	Lenvatinib은 주로 VEGFR2(KDR)/VEGFR3(Flt-4)에 대한 다중 표적 억제제이며 IC50은 4 nM/5.2 nM이고, VEGFR1/Flt-1에 대해서는 효능이 낮으며, 무세포 분석에서 FGFR1, PDGFRα/β 대비 VEGFR2/3에 대해 약 10배 더 선택적입니다. Lenvatinib (E7080)은 또한 FGFR1-4, PDGFR, Kit (c-Kit), RET (c-RET)을 억제하며 강력한 항종양 활성을 나타냅니다. 임상 3상.	Signal Transduct Target Ther, 2026, 11(1)138 Int J Biol Sci, 2026, 22(7):3617-3634 Cell Death Dis, 2026, 17(1)360
S1005	Axitinib (AG-013736)	Axitinib은 각각 Porcine aorta endothelial cells에서 0.1 nM, 0.2 nM, 0.1-0.3 nM, 1.6 nM, 1.7 nM의 IC50을 갖는 VEGFR1, VEGFR2, VEGFR3, PDGFRβ 및 c-Kit의 다중 표적 억제제입니다.	Pharmacol Res, 2026, 225:108112 Development, 2026, 153(16)dev205344 J Exp Zool B Mol Dev Evol, 2026, 346(1):7-19
S7667	SU 5402	SU5402는 IC50 값이 각각 VEGFR2에 대해 20 nM, FGFR1에 대해 30 nM, PDGF-Rβ에 대해 510 nM인 강력한 다중 표적 수용체 티로신 키나아제 억제제입니다.	Exploration (Beijing), 2026, 6(2):70160 Int J Mol Sci, 2025, 26(8)3536 Basic Clin Pharmacol Toxicol, 2025, 136(5):e70022
S8401	Erdafitinib (JNJ-42756493)	Erdafitinib은 잠재적인 항종양 활성을 가진 강력하고 선택적인 경구 투여 가능한 pan fibroblast growth factor receptor (FGFR) 억제제입니다. 이 화합물은 또한 RET (c-RET), CSF-1R, PDGFR-α/PDGFR-β, FLT4, Kit (c-Kit) 및 VEGFR-2에 결합하며 세포 apoptosis를 유도합니다.	Cell Death Dis, 2025, 16(1):868 Commun Biol, 2025, 8(1):394 Int J Mol Sci, 2025, 26(8)3525
S7397	Sorafenib (BAY 43-9006)	Sorafenib (BAY 43-9006)은 세포 무함유 분석에서 각각 6 nM 및 22 nM의 IC50을 가지는 Raf-1 및 B-Raf의 멀티키나아제 억제제입니다. Sorafenib (BAY 43-9006)은 90 nM, 20 nM, 57 nM, 59 nM 및 68 nM의 IC50으로 VEGFR-2, VEGFR-3, PDGFR-β, FLT-3 및 c-KIT을 억제합니다. Sorafenib (BAY 43-9006)은 항종양 활성과 함께 Autophagy 및 Apoptosis related 경로를 유도하고 Ferroptosis를 활성화합니다.	Signal Transduct Target Ther, 2026, 11(1)79 Int J Surg, 2026, 10.1097/JS9.0000000000004913 Acta Pharmacol Sin, 2026, 10.1038/s41401-026-01791-z
S1029	CC-5013 (Lenalidomide)	Lenalidomide는 PBMC에서 13 nM의 IC50을 갖는 TNF-alpha 분비 억제제입니다. Lenalidomide(CC-5013)는 ubiquitin E3 ligase cereblon(CRBN)의 리간드이며, CRBN-CRL4 ubiquitin ligase에 의해 두 가지 림프구 전사 인자인 IKZF1 및 IKZF3의 선택적 유비퀴틴화 및 분해를 유발합니다. Lenalidomide는 cleaved caspase-3 발현을 촉진하고 VEGF 발현을 억제하며 apoptosis를 유도합니다.	Signal Transduct Target Ther, 2025, 10(1):29 Nat Commun, 2025, 16(1):3800 Cell Rep Med, 2025, S2666-3791(25)00102-8
S1490	Ponatinib (AP24534)	Ponatinib은 Abl, PDGFRα, VEGFR2, FGFR1 및 Src에 대한 새로운 강력한 다중 표적 억제제로, 세포 없는 분석에서 각각 0.37 nM, 1.1 nM, 1.5 nM, 2.2 nM 및 5.4 nM의 IC50을 나타냅니다. Ponatinib (AP24534)은 Autophagy를 억제합니다.	Acta Pharmacol Sin, 2026, 10.1038/s41401-026-01791-z J Cell Mol Med, 2026, 30(4):e71053 Cancers (Basel), 2026, 18(7)1082
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Solid tumors require the growth and dissemination of blood vessels and lymphatic vessels to support the metastatic growth of cancers. Following the recognition of growth factor receptor pathways that regulate angiogenesis, a number of small molecular inhibitors and antibodies have been developed that target the activity of vascular endothelial growth factor (VEGF)-VEGF receptor (VEGFR) pathway. This includes oral small-molecule tyrosine kinase inhibitors currently in clinical practice, namely sunitinib and sorafenib. These are commonly used in the treatment algorithm for renal cell carcinoma (RCC) and hepatocellular carcinoma (HCC), two indications that are known to develop resistance to conventional chemotherapeutics.

The VEGFs include five known structurally-related mammalian ligands (VEGFA, VEGFB, VEGFC, VEGFD, and placenta growth factor, PLGF). The VEGFs are disulfide-bonded homodimers, however, VEGFA and PLGF heterodimers are also known to exist. Due to alternative splicing or due to processing, VEGF ligands occur as several different variants. As a result, these variants bind differently to both VEGFRs and to co-receptors resulting in different biological responses including angiogenesis, lymphangiogenesis, permeability, inflammatory cell recruitment and fatty acid uptake. VEGFs are produced by several different cell types and act in a paracrine manner. The VEGFs bind to three structurally related tyrosine kinases (VEGFR1, VEGFR2, and VEGFR3). Modulating the effect of the VEGFRs are a number of co-receptors that lack intrinsic catalytic activity (i.e. heparin sulfate, neurophilins and integrins) and bind to VEGF.^[1]

VEGFR1 (also known as Fms-like tyrosine kinase 1, Flt1, in mice) is a single-transmembrane glycoprotein structurally related to VEGFR2 and VEGFR3. VEGFR1 is expressed at high levels in vascular endothelial cells, and along with VEGFR2 binds to VEGFA. VEGFR1 is noted to bind exclusively to VEGFB and PIGF. Expression of VEGFR1 is noted to occur during vessel growth and remodeling activity. Non-endothelial cells that express VEGFR1 includes monocytes and macrophages, human tropholblasts, renal mesangial cells, vascular smooth muscle cells, dendritic cells and various tumor cells. A key regulator of VEGFR1 gene expression is hypoxia.^[1]

VEGFR2 (also known as KDR; kinase insert domain receptor, in the human and Flk1; fetal liver kinase-1, in mice) binds VEGFA with a 10-fold lower affinity than VEGFR1.  Other targets of VEGFR2 include proteolytically processed VEGFC and VEGFD. The only known ligand to uniquely bind to VEGFR2 is the open reading frame-encoded VEGFE. VEGFR2 is expressed in most adult vascular endothelial cells as well as circulating endothelial progenitor cells, pancreatic duct cells, retinal progenitor cells, megakaryocytes and hematopoietic cells. VEGFR2 expression is induced in conjunction with active angiogenesis (i.e. the uterus during the reproductive cycle) and in pathological process related to neovascularization (i.e. cancer). VEGFR2, often in combination with VEGFR3, is expressed at significantly upregulated levels in the tumor vascular endothelium in most common human solid tumors. Tumor cells can also express VEGFR2, however, epithelial and mesenchymal tumor cells typically express VEGFR1 rather than VEGFR2. Nevertheless, increased expression of VEGFR2  on tumor cells has been noted for melanoma and hematological malignancies. And, there is evidence supporting a relationship between chronic inflammation and tumor development.^[1]

VEGFR3 (also known as Fms-like tyrosine kinase 4, Flt4 in the mouse) is activated by the binding of VEGFC or VEGFD, once these two ligands undergo proteolytic processing (this increases their affinity to VEGFR2 and VEGFR3). In addition, hVEGFD shows similar affinity to both VEGFR2 and VEGFR3, while mVEGFD binds only to VEGFR3. During embryogenesis, VEGFR3 expression occurs in the primary vascular plexus at day E8.5. In late stages of embryogenesis, VEGFR3 is expressed in venous endothelial cells of the cardinal vein, that results in VEGFR3-expressing lymphatics. Postnatally, VEGFR3 plays an important role in lymphatic endothelial cells, but its expression is also observed in endothelial cells engaged in active angiogenesis, such as tumor vessels, in endothelial tip cells of angiogenic sprouts in the developing retina or in chronic inflammatory wounds. The receptor is also found in non-endothelial cells such as osteoblasts, neuronal progenitors and macrophages – all of which may indirectly support angiogenesis. It remains unclear if tumor cells express VEGFR3. Despite this lack of clarity, inhibiting VEGFR3 activity is associated with the arrest of tumor vascularization, resulting in decreased vascular density in several tumor models.^[1]

Since the VEGF-VEGFR pathway plays a significant role in angiogenesis, and it is widely known that VEGF is highly expressed in tumor and stromal cells, especially in the inflammatory cells of human tumors, dozens of angiogenesis inhibitors are currently undergoing clinical trials.^[2] However, despite the number of compounds that has been identified for targeting the VEGF-VEGFR pathway, there is a high attrition rate. Several challenges in the development of angiogenesis inhibitors relate to their specificity, efficacy, side effects, and resistance to anti-angiogenic tumor therapy. However, the emergence of personalized medicine – based on the use of biomarkers – will likely lead to the identification of patient populations that is likely to define respondent groups.