Bifunctional Fusion(双功能融合)研究综述
Bifunctional Fusion 双功能融合 - In this phase II study, we will investigate the feasibility of addition of bintrafusp alfa, a bifunctional fusion protein blocking TGF-β and PD-L1, to definitive chemoradiation in patients with esophageal squamous cell carcinoma. [1] Bintrafusp alfa is a bifunctional fusion p. [2] To this end, multiple structures on tumor vascular wall cells have been studied at which tTF has been aimed via antibodies, derivatives, or as bifunctional fusion protein through targeting peptides. [3] In the present study, bifunctional fusion proteins were designed by fusing the kringle 2 and protease domains of tissue-type plasminogen activator (tPA) to the C-terminal fragment of hirudin. [4] Bintrafusp alfa (M7824) is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor, functioning as a TGF-β “trap”, fused to a human IgG1 antibody blocking PD-L1. [5] Here, we assessed SHR-1701, a novel bifunctional fusion protein composed of a mAb against PD-L1 fused with the extracellular domain of TGF-β receptor II, in advanced NSCLC pts including one separate EGFR+ cohort. [6] AMG 256 is a bifunctional fusion protein comprising a PD-1-targeting antibody and IL-21 mutein designed to deliver IL-21 pathway stimulation to PD-1+ cells—a strategy that is designed to prime and extend the activity of cytotoxic and memory T cells and induce anti-tumor immunity. [7] 1 demonstrate that a bifunctional fusion protein targeting TGF-β and PD-L1 can synergize with radiation therapy to simultaneously augment tumor control and reduce normal tissue toxicity. [8] Further synergy has been shown with a novel first-in-class bifunctional fusion protein (bintrafusp alfa) composed of the extracellular domain of human TGF-β receptor II (TGFβRII), which effectively functions to sequester or “trap” all three TGF-β isoforms (Lind H, JITC 2020), fused to a monoclonal antibody against PD-L1. [9] Specifically, we developed a bifunctional fusion protein consisting of a cellulose-binding domain and a nanobody (Nb) targeting the receptor-binding domain of SARS-CoV-2. [10] We armed MDRVV with a bifunctional fusion gene encoding cytosine deaminase and uracil phosphoribosyltransferase (CD/UPRT), which converts 5-fluorocytosine (5-FC) into chemotherapeutic agents, and evaluated its oncolytic activity alone or in combination with 5-FC in human pancreatic cancer cell lines, tumor mouse models of peritoneal dissemination and liver metastasis, and ex vivo-infected live pancreatic cancer patient-derived tissues. [11] AIMS To engineer and screen a novel GLP-1/anti-apolipoprotein B (apoB) bifunctional fusion protein with therapeutic potential on alleviating diabetes and diabetic complication in combination with low-intensity ultrasound. [12] TST005 is a bifunctional fusion protein composed of the truncated extracellular domain of the TGF-βRII receptor (a TGF-β trap) fused to a humanized anti-PD-L1 IgG1 antibody (AM4B6 mAb) with ablated Fc immune effector function. [13] 6020 Background: Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [14] To tune the efficiency of oxidized cofactor recycling between alcohol dehydrogenase (ADH) and NADH oxidase (NOX) for the production of aromatic chiral alcohols, we designed and constructed four novel bifunctional fusion proteins composed of thermostable ADH and NOX from Thermococcus kodakarensis KOD1. [15] Our results reveal that the bifunctional fusion protein vmab-mIL22 can trigger potent therapeutic effects in H1N1-infected mice by enhancing lung tissue recovery and inhibiting pulmonary inflammation, which highlights a potential approach for treating influenza A virus infection by targeting IL-17A and IL-22 simultaneously. [16] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 antibody blocking PD-L1. [17] To address this, we used both a small molecule TGFβ inhibitor in combination with anti-PD-L1 and a bifunctional fusion protein targeting both TGFβ and PD-L1 to treat mouse SCCs and found TGFβ inhibition enhanced PD-L1 blockade-induced tumor eradication in multiple tumor models. [18] We report that a bifunctional fusion protein that simultaneously inhibits TGF-β and PD-L1, bintrafusp alfa (BA), effectively synergizes with radiotherapy, leading to superior survival in multiple therapy-resistant murine tumor models with poor immune infiltration. [19] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGFβ receptor II (TGFβRII) (a TGFβ “trap”) fused to a human IgG1 monoclonal antibody blocking PD-L1. [20] Here we describe the creation of a heterodimeric bifunctional fusion molecule, HCW9218, constructed using our soluble tissue factor-based scaffold technology. [21] Bintrafusp alfa is a bifunctional fusion protein, which blocks PD-L1 and sequesters TGF-b from the systemic circulation via a TGF-bRII component, offering. [22] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [23] Moreover, bifunctional fusion proteins of αTAA–tumor necrosis factor ligand (TNFL) superfamily members including 4-1BBL, OX40L, CD70 and TL1A have been tested. [24] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [25] The immune effects of the bifunctional fusion protein on myeloid cells in the tumor mass and draining lymph nodes were analyzed by flow cytometry. [26] Bintrafusp alfa, a first-in-class bifunctional fusion protein composed of the extracellular domain of the human transforming growth factor β receptor II (TGF-βRII or TGF-β “trap”) fused to the heavy chain of an IgG1 antibody blocking programmed death ligand 1 (anti-PDL1), was designed to target two key immunosuppressive pathways in the tumor microenvironment (TME). [27] IntroductionBintrafusp alfa, an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 monoclonal antibody blocking programmed death ligand 1, has shown promising antitumor activity and manageable safety. [28] Also, a strategy was developed for bioconjugation of antibodies onto the surface of the PS-UCNPs by using the bifunctional fusion protein linker-protein G (LPG). [29] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [30] E1A) was an attractive transfer system that preferentially homing and treating cancer metastasis, through which the tumor cells were modified by locally replicated adenoviruses to release CD3-HAC, a bifunctional fusion protein that anti-CD3 scfv linked with high-affinity consensus (HAC) PD-1. [31] M7824 is an innovative first-in-class bifunctional fusion protein composed of two extracellular domains of TGF-βRII (a TGF-β “trap”) fused with a human IgG1 monoclonal antibody against PD-L1. [32] Furthermore, corroborating the concept, OX40L and GITRL were also successfully incorporated into the novel single-chain format and the advantage of target-bound trifunctional versus corresponding combined bifunctional fusion proteins demonstrated by measuring T-cell proliferation and cytotoxic potential in vitro and antitumor effects of RD_IL15_scFv_scGITRL in a lung tumor mouse model in vivo. [33] M7824 is an innovative first-in-class bifunctional fusion protein co. [34] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β ‘trap’) fused to a human IgG1 mAb blocking PD-L1. [35] Linker-protein G (LPG) is a bifunctional fusion protein composed of a solid-binding peptide (SBP, referred as the “linker”) with high affinity to silica-based compounds and a Streptococcus protein G (PG), which binds antibodies. [36] Taken together, the present study provides a new approach of using bifunctional fusion proteins to target both angiogenesis and T lymphocyte activation for cancer therapy. [37] M7824 is an innovative first-in-class bifunctional fusion protein composed of 2 extracellular domains of TGF-βRII (a TGF-β “trap”) fused to a human IgG1 mAb against PD-L1. [38] ABSTRACT Here we describe a novel bifunctional fusion protein, designated N-809. [39]在这项 II 期研究中，我们将研究在食管鳞状细胞癌患者的根治性放化疗中添加 bintrafusp alfa（一种阻断 TGF-β 和 PD-L1 的双功能融合蛋白）的可行性。 [1] Bintrafusp alpha 是一种双功能融合 p。 [2] 为此，已经研究了肿瘤血管壁细胞上的多种结构，其中 tTF 已通过抗体、衍生物或通过靶向肽作为双功能融合蛋白来瞄准。 [3] 在本研究中，通过将组织型纤溶酶原激活物 (tPA) 的三环 2 和蛋白酶结构域与水蛭素的 C 末端片段融合设计了双功能融合蛋白。 [4] Bintrafusp alfa (M7824) 是一种一流的双功能融合蛋白，由 TGF-βRII 受体的细胞外结构域组成，充当 TGF-β“陷阱”，与阻断 PD-L1 的人 IgG1 抗体融合。 [5] 在这里，我们评估了 SHR-1701，这是一种新型双功能融合蛋白，由一种针对 PD-L1 的 mAb 与 TGF-β 受体 II 的细胞外结构域融合而成，用于晚期 NSCLC 患者，包括一个单独的 EGFR+ 队列。 [6] AMG 256 是一种双功能融合蛋白，包含一种 PD-1 靶向抗体和 IL-21 突变蛋白，旨在将 IL-21 通路刺激传递给 PD-1+ 细胞——一种旨在启动和延长细胞毒性和记忆活性的策略T 细胞并诱导抗肿瘤免疫。 [7] 图 1 表明靶向 TGF-β 和 PD-L1 的双功能融合蛋白可以与放射治疗协同作用，同时增强肿瘤控制并降低正常组织毒性。 [8] 由人 TGF-β 受体 II (TGFβRII) 的细胞外结构域组成的新型一流双功能融合蛋白 (bintrafusp alfa) 显示出进一步的协同作用，可有效隔离或“捕获”所有三种 TGF-β亚型 (Lind H, JITC 2020)，与针对 PD-L1 的单克隆抗体融合。 [9] 具体来说，我们开发了一种由纤维素结合域和靶向 SARS-CoV-2 受体结合域的纳米抗体 (Nb) 组成的双功能融合蛋白。 [10] 我们用编码胞嘧啶脱氨酶和尿嘧啶磷酸核糖基转移酶 (CD/UPRT) 的双功能融合基因武装 MDRVV，将 5-氟胞嘧啶 (5-FC) 转化为化疗剂，并评估其单独或与 5-FC 在人胰腺中的溶瘤活性癌细胞系，腹膜传播和肝转移的肿瘤小鼠模型，以及离体感染的活胰腺癌患者来源的组织。 [11] 目标 设计和筛选一种新型 GLP-1/抗载脂蛋白 B (apoB) 双功能融合蛋白，结合低强度超声具有缓解糖尿病和糖尿病并发症的治疗潜力。 [12] TST005 是一种双功能融合蛋白，由 TGF-βRII 受体（一种 TGF-β 陷阱）的截短细胞外结构域与具有消融 Fc 免疫效应功能的人源化抗 PD-L1 IgG1 抗体（AM4B6 mAb）融合而成。 [13] 6020 背景：Bintrafusp alfa 是一流的双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [14] 为了调整醇脱氢酶 (ADH) 和 NADH 氧化酶 (NOX) 之间氧化辅因子再循环的效率以生产芳香手性醇，我们设计并构建了四种新型双功能融合蛋白，由来自 Thermococcus kodakarensis KOD1 的热稳定 ADH 和 NOX 组成。 [15] 我们的研究结果表明，双功能融合蛋白 vmab-mIL22 可以通过增强肺组织恢复和抑制肺部炎症来触发 H1N1 感染小鼠的有效治疗效果，这突出了通过靶向 IL-17A 和 IL- 治疗甲型流感病毒感染的潜在方法22 同时。 [16] nan [17] 为了解决这个问题，我们使用小分子 TGFβ 抑制剂联合抗 PD-L1 和靶向 TGFβ 和 PD-L1 的双功能融合蛋白来治疗小鼠 SCC，发现 TGFβ 抑制增强了 PD-L1 阻断诱导的肿瘤根除多种肿瘤模型。 [18] 我们报告了一种同时抑制 TGF-β 和 PD-L1 的双功能融合蛋白 bintrafusp alfa (BA)，可有效地与放射疗法协同作用，从而在免疫浸润较差的多种抗治疗小鼠肿瘤模型中获得更高的存活率。 [19] nan [20] nan [21] Bintrafusp alfa 是一种双功能融合蛋白，可通过 TGF-bRII 成分阻断 PD-L1 并从体循环中隔离 TGF-b。 [22] nan [23] 此外，还测试了 αTAA-肿瘤坏死因子配体 (TNFL) 超家族成员的双功能融合蛋白，包括 4-1BBL、OX40L、CD70 和 TL1A。 [24] nan [25] 通过流式细胞术分析双功能融合蛋白对肿瘤块和引流淋巴结中的骨髓细胞的免疫作用。 [26] nan [27] 引言Bintrafusp alfa 是一种创新的一流双功能融合蛋白，由与阻断程序性死亡配体 1 的人 IgG1 单克隆抗体融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成，已显示出有前景的抗肿瘤作用活动和可管理的安全性。 [28] 此外，还开发了一种通过使用双功能融合蛋白接头-蛋白 G (LPG) 将抗体生物偶联到 PS-UCNPs 表面的策略。 [29] Bintrafusp alfa* (M7824) 是一种创新的一流双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [30] E1A) 是一种有吸引力的转移系统，它优先归巢和治疗癌症转移，通过该系统，肿瘤细胞被局部复制的腺病毒修饰以释放 CD3-HAC，这是一种双功能融合蛋白，抗 CD3 scfv 与高亲和力共识 (HAC) 相关联PD-1。 [31] nan [32] nan [33] nan [34] nan [35] 接头蛋白 G (LPG) 是一种双功能融合蛋白，由对二氧化硅基化合物具有高亲和力的固体结合肽 (SBP，称为“接头”) 和与抗体结合的链球菌蛋白 G (PG) 组成。 [36] 总之，本研究提供了一种使用双功能融合蛋白靶向血管生成和 T 淋巴细胞活化以进行癌症治疗的新方法。 [37] nan [38] nan [39]
trap ” fused 陷阱”融合
Bintrafusp alfa (M7824) is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor, functioning as a TGF-β “trap”, fused to a human IgG1 antibody blocking PD-L1. [1] 6020 Background: Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [2] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 antibody blocking PD-L1. [3] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGFβ receptor II (TGFβRII) (a TGFβ “trap”) fused to a human IgG1 monoclonal antibody blocking PD-L1. [4] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [5] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [6] Bintrafusp alfa, a first-in-class bifunctional fusion protein composed of the extracellular domain of the human transforming growth factor β receptor II (TGF-βRII or TGF-β “trap”) fused to the heavy chain of an IgG1 antibody blocking programmed death ligand 1 (anti-PDL1), was designed to target two key immunosuppressive pathways in the tumor microenvironment (TME). [7] IntroductionBintrafusp alfa, an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 monoclonal antibody blocking programmed death ligand 1, has shown promising antitumor activity and manageable safety. [8] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [9] M7824 is an innovative first-in-class bifunctional fusion protein composed of two extracellular domains of TGF-βRII (a TGF-β “trap”) fused with a human IgG1 monoclonal antibody against PD-L1. [10] M7824 is an innovative first-in-class bifunctional fusion protein composed of 2 extracellular domains of TGF-βRII (a TGF-β “trap”) fused to a human IgG1 mAb against PD-L1. [11]Bintrafusp alfa (M7824) 是一种一流的双功能融合蛋白，由 TGF-βRII 受体的细胞外结构域组成，充当 TGF-β“陷阱”，与阻断 PD-L1 的人 IgG1 抗体融合。 [1] 6020 背景：Bintrafusp alfa 是一流的双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [2] nan [3] nan [4] nan [5] nan [6] nan [7] 引言Bintrafusp alfa 是一种创新的一流双功能融合蛋白，由与阻断程序性死亡配体 1 的人 IgG1 单克隆抗体融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成，已显示出有前景的抗肿瘤作用活动和可管理的安全性。 [8] Bintrafusp alfa* (M7824) 是一种创新的一流双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [9] nan [10] nan [11]
Clas Bifunctional Fusion Clas 双功能融合
Bintrafusp alfa (M7824) is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor, functioning as a TGF-β “trap”, fused to a human IgG1 antibody blocking PD-L1. [1] Further synergy has been shown with a novel first-in-class bifunctional fusion protein (bintrafusp alfa) composed of the extracellular domain of human TGF-β receptor II (TGFβRII), which effectively functions to sequester or “trap” all three TGF-β isoforms (Lind H, JITC 2020), fused to a monoclonal antibody against PD-L1. [2] 6020 Background: Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [3] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 antibody blocking PD-L1. [4] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGFβ receptor II (TGFβRII) (a TGFβ “trap”) fused to a human IgG1 monoclonal antibody blocking PD-L1. [5] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [6] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [7] Bintrafusp alfa, a first-in-class bifunctional fusion protein composed of the extracellular domain of the human transforming growth factor β receptor II (TGF-βRII or TGF-β “trap”) fused to the heavy chain of an IgG1 antibody blocking programmed death ligand 1 (anti-PDL1), was designed to target two key immunosuppressive pathways in the tumor microenvironment (TME). [8] IntroductionBintrafusp alfa, an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 monoclonal antibody blocking programmed death ligand 1, has shown promising antitumor activity and manageable safety. [9] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [10] M7824 is an innovative first-in-class bifunctional fusion protein composed of two extracellular domains of TGF-βRII (a TGF-β “trap”) fused with a human IgG1 monoclonal antibody against PD-L1. [11] M7824 is an innovative first-in-class bifunctional fusion protein co. [12] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β ‘trap’) fused to a human IgG1 mAb blocking PD-L1. [13] M7824 is an innovative first-in-class bifunctional fusion protein composed of 2 extracellular domains of TGF-βRII (a TGF-β “trap”) fused to a human IgG1 mAb against PD-L1. [14]Bintrafusp alfa (M7824) 是一种一流的双功能融合蛋白，由 TGF-βRII 受体的细胞外结构域组成，充当 TGF-β“陷阱”，与阻断 PD-L1 的人 IgG1 抗体融合。 [1] 由人 TGF-β 受体 II (TGFβRII) 的细胞外结构域组成的新型一流双功能融合蛋白 (bintrafusp alfa) 显示出进一步的协同作用，可有效隔离或“捕获”所有三种 TGF-β亚型 (Lind H, JITC 2020)，与针对 PD-L1 的单克隆抗体融合。 [2] 6020 背景：Bintrafusp alfa 是一流的双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [3] nan [4] nan [5] nan [6] nan [7] nan [8] 引言Bintrafusp alfa 是一种创新的一流双功能融合蛋白，由与阻断程序性死亡配体 1 的人 IgG1 单克隆抗体融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成，已显示出有前景的抗肿瘤作用活动和可管理的安全性。 [9] Bintrafusp alfa* (M7824) 是一种创新的一流双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [10] nan [11] nan [12] nan [13] nan [14]
Novel Bifunctional Fusion 新型双功能融合
Here, we assessed SHR-1701, a novel bifunctional fusion protein composed of a mAb against PD-L1 fused with the extracellular domain of TGF-β receptor II, in advanced NSCLC pts including one separate EGFR+ cohort. [1] To tune the efficiency of oxidized cofactor recycling between alcohol dehydrogenase (ADH) and NADH oxidase (NOX) for the production of aromatic chiral alcohols, we designed and constructed four novel bifunctional fusion proteins composed of thermostable ADH and NOX from Thermococcus kodakarensis KOD1. [2] ABSTRACT Here we describe a novel bifunctional fusion protein, designated N-809. [3]在这里，我们评估了 SHR-1701，这是一种新型双功能融合蛋白，由一种针对 PD-L1 的 mAb 与 TGF-β 受体 II 的细胞外结构域融合而成，用于晚期 NSCLC 患者，包括一个单独的 EGFR+ 队列。 [1] 为了调整醇脱氢酶 (ADH) 和 NADH 氧化酶 (NOX) 之间氧化辅因子再循环的效率以生产芳香手性醇，我们设计并构建了四种新型双功能融合蛋白，由来自 Thermococcus kodakarensis KOD1 的热稳定 ADH 和 NOX 组成。 [2] nan [3]
bifunctional fusion protein 双功能融合蛋白
In this phase II study, we will investigate the feasibility of addition of bintrafusp alfa, a bifunctional fusion protein blocking TGF-β and PD-L1, to definitive chemoradiation in patients with esophageal squamous cell carcinoma. [1] To this end, multiple structures on tumor vascular wall cells have been studied at which tTF has been aimed via antibodies, derivatives, or as bifunctional fusion protein through targeting peptides. [2] In the present study, bifunctional fusion proteins were designed by fusing the kringle 2 and protease domains of tissue-type plasminogen activator (tPA) to the C-terminal fragment of hirudin. [3] Bintrafusp alfa (M7824) is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor, functioning as a TGF-β “trap”, fused to a human IgG1 antibody blocking PD-L1. [4] Here, we assessed SHR-1701, a novel bifunctional fusion protein composed of a mAb against PD-L1 fused with the extracellular domain of TGF-β receptor II, in advanced NSCLC pts including one separate EGFR+ cohort. [5] AMG 256 is a bifunctional fusion protein comprising a PD-1-targeting antibody and IL-21 mutein designed to deliver IL-21 pathway stimulation to PD-1+ cells—a strategy that is designed to prime and extend the activity of cytotoxic and memory T cells and induce anti-tumor immunity. [6] 1 demonstrate that a bifunctional fusion protein targeting TGF-β and PD-L1 can synergize with radiation therapy to simultaneously augment tumor control and reduce normal tissue toxicity. [7] Further synergy has been shown with a novel first-in-class bifunctional fusion protein (bintrafusp alfa) composed of the extracellular domain of human TGF-β receptor II (TGFβRII), which effectively functions to sequester or “trap” all three TGF-β isoforms (Lind H, JITC 2020), fused to a monoclonal antibody against PD-L1. [8] Specifically, we developed a bifunctional fusion protein consisting of a cellulose-binding domain and a nanobody (Nb) targeting the receptor-binding domain of SARS-CoV-2. [9] AIMS To engineer and screen a novel GLP-1/anti-apolipoprotein B (apoB) bifunctional fusion protein with therapeutic potential on alleviating diabetes and diabetic complication in combination with low-intensity ultrasound. [10] TST005 is a bifunctional fusion protein composed of the truncated extracellular domain of the TGF-βRII receptor (a TGF-β trap) fused to a humanized anti-PD-L1 IgG1 antibody (AM4B6 mAb) with ablated Fc immune effector function. [11] 6020 Background: Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [12] To tune the efficiency of oxidized cofactor recycling between alcohol dehydrogenase (ADH) and NADH oxidase (NOX) for the production of aromatic chiral alcohols, we designed and constructed four novel bifunctional fusion proteins composed of thermostable ADH and NOX from Thermococcus kodakarensis KOD1. [13] Our results reveal that the bifunctional fusion protein vmab-mIL22 can trigger potent therapeutic effects in H1N1-infected mice by enhancing lung tissue recovery and inhibiting pulmonary inflammation, which highlights a potential approach for treating influenza A virus infection by targeting IL-17A and IL-22 simultaneously. [14] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 antibody blocking PD-L1. [15] To address this, we used both a small molecule TGFβ inhibitor in combination with anti-PD-L1 and a bifunctional fusion protein targeting both TGFβ and PD-L1 to treat mouse SCCs and found TGFβ inhibition enhanced PD-L1 blockade-induced tumor eradication in multiple tumor models. [16] We report that a bifunctional fusion protein that simultaneously inhibits TGF-β and PD-L1, bintrafusp alfa (BA), effectively synergizes with radiotherapy, leading to superior survival in multiple therapy-resistant murine tumor models with poor immune infiltration. [17] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGFβ receptor II (TGFβRII) (a TGFβ “trap”) fused to a human IgG1 monoclonal antibody blocking PD-L1. [18] Bintrafusp alfa is a bifunctional fusion protein, which blocks PD-L1 and sequesters TGF-b from the systemic circulation via a TGF-bRII component, offering. [19] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [20] Moreover, bifunctional fusion proteins of αTAA–tumor necrosis factor ligand (TNFL) superfamily members including 4-1BBL, OX40L, CD70 and TL1A have been tested. [21] Bintrafusp alfa is a first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [22] The immune effects of the bifunctional fusion protein on myeloid cells in the tumor mass and draining lymph nodes were analyzed by flow cytometry. [23] Bintrafusp alfa, a first-in-class bifunctional fusion protein composed of the extracellular domain of the human transforming growth factor β receptor II (TGF-βRII or TGF-β “trap”) fused to the heavy chain of an IgG1 antibody blocking programmed death ligand 1 (anti-PDL1), was designed to target two key immunosuppressive pathways in the tumor microenvironment (TME). [24] IntroductionBintrafusp alfa, an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 monoclonal antibody blocking programmed death ligand 1, has shown promising antitumor activity and manageable safety. [25] Also, a strategy was developed for bioconjugation of antibodies onto the surface of the PS-UCNPs by using the bifunctional fusion protein linker-protein G (LPG). [26] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β “trap”) fused to a human IgG1 mAb blocking PD-L1. [27] E1A) was an attractive transfer system that preferentially homing and treating cancer metastasis, through which the tumor cells were modified by locally replicated adenoviruses to release CD3-HAC, a bifunctional fusion protein that anti-CD3 scfv linked with high-affinity consensus (HAC) PD-1. [28] M7824 is an innovative first-in-class bifunctional fusion protein composed of two extracellular domains of TGF-βRII (a TGF-β “trap”) fused with a human IgG1 monoclonal antibody against PD-L1. [29] Furthermore, corroborating the concept, OX40L and GITRL were also successfully incorporated into the novel single-chain format and the advantage of target-bound trifunctional versus corresponding combined bifunctional fusion proteins demonstrated by measuring T-cell proliferation and cytotoxic potential in vitro and antitumor effects of RD_IL15_scFv_scGITRL in a lung tumor mouse model in vivo. [30] M7824 is an innovative first-in-class bifunctional fusion protein co. [31] Bintrafusp alfa* (M7824) is an innovative first-in-class bifunctional fusion protein composed of the extracellular domain of the TGF-βRII receptor (a TGF-β ‘trap’) fused to a human IgG1 mAb blocking PD-L1. [32] Linker-protein G (LPG) is a bifunctional fusion protein composed of a solid-binding peptide (SBP, referred as the “linker”) with high affinity to silica-based compounds and a Streptococcus protein G (PG), which binds antibodies. [33] Taken together, the present study provides a new approach of using bifunctional fusion proteins to target both angiogenesis and T lymphocyte activation for cancer therapy. [34] M7824 is an innovative first-in-class bifunctional fusion protein composed of 2 extracellular domains of TGF-βRII (a TGF-β “trap”) fused to a human IgG1 mAb against PD-L1. [35] ABSTRACT Here we describe a novel bifunctional fusion protein, designated N-809. [36]在这项 II 期研究中，我们将研究在食管鳞状细胞癌患者的根治性放化疗中添加 bintrafusp alfa（一种阻断 TGF-β 和 PD-L1 的双功能融合蛋白）的可行性。 [1] 为此，已经研究了肿瘤血管壁细胞上的多种结构，其中 tTF 已通过抗体、衍生物或通过靶向肽作为双功能融合蛋白来瞄准。 [2] 在本研究中，通过将组织型纤溶酶原激活物 (tPA) 的三环 2 和蛋白酶结构域与水蛭素的 C 末端片段融合设计了双功能融合蛋白。 [3] Bintrafusp alfa (M7824) 是一种一流的双功能融合蛋白，由 TGF-βRII 受体的细胞外结构域组成，充当 TGF-β“陷阱”，与阻断 PD-L1 的人 IgG1 抗体融合。 [4] 在这里，我们评估了 SHR-1701，这是一种新型双功能融合蛋白，由一种针对 PD-L1 的 mAb 与 TGF-β 受体 II 的细胞外结构域融合而成，用于晚期 NSCLC 患者，包括一个单独的 EGFR+ 队列。 [5] AMG 256 是一种双功能融合蛋白，包含一种 PD-1 靶向抗体和 IL-21 突变蛋白，旨在将 IL-21 通路刺激传递给 PD-1+ 细胞——一种旨在启动和延长细胞毒性和记忆活性的策略T 细胞并诱导抗肿瘤免疫。 [6] 图 1 表明靶向 TGF-β 和 PD-L1 的双功能融合蛋白可以与放射治疗协同作用，同时增强肿瘤控制并降低正常组织毒性。 [7] 由人 TGF-β 受体 II (TGFβRII) 的细胞外结构域组成的新型一流双功能融合蛋白 (bintrafusp alfa) 显示出进一步的协同作用，可有效隔离或“捕获”所有三种 TGF-β亚型 (Lind H, JITC 2020)，与针对 PD-L1 的单克隆抗体融合。 [8] 具体来说，我们开发了一种由纤维素结合域和靶向 SARS-CoV-2 受体结合域的纳米抗体 (Nb) 组成的双功能融合蛋白。 [9] 目标 设计和筛选一种新型 GLP-1/抗载脂蛋白 B (apoB) 双功能融合蛋白，结合低强度超声具有缓解糖尿病和糖尿病并发症的治疗潜力。 [10] TST005 是一种双功能融合蛋白，由 TGF-βRII 受体（一种 TGF-β 陷阱）的截短细胞外结构域与具有消融 Fc 免疫效应功能的人源化抗 PD-L1 IgG1 抗体（AM4B6 mAb）融合而成。 [11] 6020 背景：Bintrafusp alfa 是一流的双功能融合蛋白，由与阻断 PD-L1 的人 IgG1 mAb 融合的 TGF-βRII 受体（TGF-β“陷阱”）的细胞外结构域组成。 [12] 为了调整醇脱氢酶 (ADH) 和 NADH 氧化酶 (NOX) 之间氧化辅因子再循环的效率以生产芳香手性醇，我们设计并构建了四种新型双功能融合蛋白，由来自 Thermococcus kodakarensis KOD1 的热稳定 ADH 和 NOX 组成。 [13] 我们的研究结果表明，双功能融合蛋白 vmab-mIL22 可以通过增强肺组织恢复和抑制肺部炎症来触发 H1N1 感染小鼠的有效治疗效果，这突出了通过靶向 IL-17A 和 IL- 治疗甲型流感病毒感染的潜在方法22 同时。 [14] nan