Monosodium Glutamate (MSG) is an amino acid salt that naturally enhances umami taste in many foods. It is often used to reduce salt (NaCl) in products while keeping the flavour. However, MSG might slow down satiation, leading to larger portions. This effect could vary based on diet and umami exposure, but there is no empirical data yet to confirm this hypothesis. Therefore, a long-term systematic investigation is necessary to objectively evaluate what the duration and extent of the effect of umami taste exposure is on absolute food intake, and whether it can have an effect on other outcomes, such as appetite ratings, meal liking, taste sensitivity, food preference, body hydration, weight status, self-reported diet tolerance and other potential side effects. The study sample will consist of 75 participants, that will randomly be distributed over three intervention groups: regular umami exposure (n = 25), low umami exposure (n = 25) and high umami exposure (n = 25). The intervention is fully controlled, for a period of two weeks, with an additional one-week run-in period in which all participants consume the regular umami exposure diet. Umami taste will be added through MSG supplementation of the three main meals. Supplementation will depend on both intervention group, and individual participants' body weight. The primary objective is to compare the effects of a 2-week low-, regular- and high dietary MSG exposure on umami-induced satiation. Differences in absolute food intake will be assessed by an ad libitum satiation test, which participants will be presented with at baseline (day 7), mid-intervention (day 14) and end of intervention (day 22). Secondary outcomes such as differences between intervention groups in satiety and appetite ratings, test meal liking, taste sensitivity, food preference, body hydration status, weight, self-reported diet tolerance and other potential side effects.

开始日期2025-09-01

申办/合作机构

Wageningen University

[+1]

CTR20244331

/ Recruiting临床3期

在免疫球蛋白 A 肾病成人患者中评价 POVETACICEPT 的随机、双盲、安慰剂对照 III 期研究（RAINIER）

主要目的（主队列）评价 Povetacicept 与安慰剂相比在减少蛋白尿方面的疗效评价 Povetacicept 与安慰剂相比在保护肾功能方面的疗效次要目的（主队列）评价 Povetacicept 与安慰剂相比在减缓肾衰竭方面的疗效评价 Povetacicept 与安慰剂相比在改善疲劳方面的疗效安全性目的（主队列）评价 Povetacicept 与安慰剂相比的安全性和耐受性特征

开始日期2024-12-16

申办/合作机构

乔治（北京）临床医学研究有限公司

[+3]

CTR20243961

/ Completed临床1期

评价 Volagidemab（REMD-477）在中国健康成年受试者中单次皮下给药后的安全性、耐受性以及药代动力学的 I 期临床研究

主要目的： 1) 评价中国健康成年受试者单次皮下注射 Volagidemab 的安全性和耐受性。次要目的： 1) 评价中国健康成年受试者单次皮下注射 Volagidemab 后体内的药代动力学（PK）特征和药效学（PD）。 2) 探索中国健康成年受试者单次皮下注射 Volagidemab 后对肝功能的影响。 3) 评价中国健康成年受试者单次皮下注射 Volagidemab 后的免疫原性。

开始日期2024-11-22

申办/合作机构

北京科信美德生物医药科技有限公司

[+2]

100 项与 Ajinomoto Co., Inc. 相关的临床结果

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0 项与 Ajinomoto Co., Inc. 相关的专利（医药）

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2,498

项与 Ajinomoto Co., Inc. 相关的文献（医药）

2025-08-20·BIOCONJUGATE CHEMISTRY

Harnessing Fc-Directed Bioconjugation for the Synthesis of Site-Specifically Modified Radioimmunoconjugates

Article

作者: McGlone, Shane A. ; Watanabe, Tomohiro ; Zeglis, Brian M. ; Sebastiano, Joni ; Grimaldi, Camilla ; Fujii, Tomohiro ; Kao, Wei-Siang Mark ; Aoki, Tsubasa ; Strugala, Emilia

A growing body of preclinical and clinical evidence has shown that site-specifically and site-selectively modified immunoconjugates exhibit improved in vivo performance compared to their stochastically modified cousins. However, extant approaches to site-specific bioconjugation suffer from a variety of issues that make clinical translation challenging, including instability, complexity, and expense. Herein, we describe a novel chemical approach to the synthesis of site-specifically modified radioimmunoconjugates that is simple and straightforward. To this end, we leveraged an Fc-directed peptide to append free sulfhydryl moieties to unique sites within the Fc domain of the CA19-9-targeting antibody 5B1. These thiols were then modified with phenyloxadiazolyl methylsulfone-bearing variants of the chelator CHX-A″-DTPA, and the immunoconjugate was radiolabeled with [¹⁷⁷Lu]Lu³⁺ to produce [¹⁷⁷Lu]Lu-DTPA-^PODSAJICAP-5B1 in high yield, purity, and specific activity. Subsequent analyses confirmed the site-specificity of the modification and demonstrated the high stability and immunoreactivity of the radioimmunoconjugate. Biodistribution studies in athymic nude mice bearing subcutaneous BxPC3 pancreatic cancer xenografts revealed that [¹⁷⁷Lu]Lu-DTPA-^PODSAJICAP-5B1 produced high activity concentrations in tumor tissue as well as high tumor-to-background activity concentration ratios and displayed performance that compared favorably to ¹⁷⁷Lu-labeled analogues synthesized with traditional stochastic and thiol-selective bioconjugation strategies.

2025-07-10·ACS Medicinal Chemistry Letters

Homogeneous Dual-Payload Antibody-Drug Conjugates Produced by Combined Distinct Conjugation Strategies

Article

作者: Fujii, Tomohiro ; Matsuda, Yutaka ; Iwai, Yusuke ; Seki, Takuya ; Watanabe, Tomohiro ; Stofleth, Jason T.

Antibody-drug conjugates (ADCs) represent a promising class of targeted cancer therapies, combining monoclonal antibody specificity with cytotoxic drug potency. Despite significant ADC technology advancements, challenges such as limited efficacy, often attributed to tumor heterogeneity and resistance development, remain present. In this study, we developed homogeneous dual-payload ADCs by combining site-selective conjugation methods: second-generation AJICAP technology for lysine modification and conventional interchain-break conjugation. Using trastuzumab as a model antibody, we successfully synthesized a drug-to-antibody ratio (DAR) of 10 (2 + 8) dual-payload ADC with monomethyl auristatin E and deruxtecan, displaying low aggregation and stable physicochemical properties. The dual-payload ADC exhibited superior in vitro cytotoxicity against HER2-positive SKBR-3 cells, compared to T-DXd, and demonstrated enhanced tumor suppression in vivo in a NCI-N87 xenograft model. These results highlight the potential of multipayload ADCs in enhancing therapeutic efficacy while maintaining stability, thereby providing a new strategy to overcome traditional ADC-related limitations.

2025-07-01·ARCHIVES OF MICROBIOLOGY

The mechanism of action of nisin in promoting poultry through tight junction integrity and dendritic cell anti-inflammatory properties

Article

作者: Uehara, Akinori ; Maekawa, Mayumi ; Nakagawa, Kazuki

Antimicrobial resistance in microbes poses a global health threat, making the search for alternatives to antibiotic growth promoters (AGPs) in the livestock industry an urgent priority. Nisin, an antibacterial peptide widely used as a food preservative, can enhance the poultry growth performance. However, its efficacy requires high doses owing to its degradation by digestive enzymes. Moreover, the mechanisms underlying its effect remain unclear. We investigated the effects of nisin on antimicrobial activity, tight junction integrity, and anti-inflammatory response using intestinal microorganisms, epithelial cells, and immune cells. Nisin displayed broad antibacterial activity against Gram-positive bacteria, including both pathogenic and beneficial species such as lactic acid bacteria. In contrast, Gram-negative bacteria, such as Escherichia coli and Salmonella, were highly resistant to nisin. Moreover, nisin improved tight junction integrity at concentrations over 100 times lower than those required for antimicrobial activity. In addition, nisin reduced inflammation-related cytokines, including TNF-α, IL-1β, IL-6, and IL-12p70, secreted by dendritic cells at concentrations over five times lower than those needed for antimicrobial activity. Furthermore, the prototype of the enteric-coated nisin was effective under a state of dynamic equilibrium in the dissolution tests. Notably, nisin improved tight junction integrity at low concentrations, comparable to those of AGPs. Therefore, the results suggest that the growth-promoting effect of nisin is not due to antimicrobial action but rather to its ability to enhance tight junction integrity and reduce inflammation of dendritic cells, making it a potential alternative to AGPs without the risk of superbug emergence.

158

项与 Ajinomoto Co., Inc. 相关的新闻（医药）

2025-08-22

·生物制品圈

人凝血酶原复合物的分离纯化工艺

中文摘要目的探究应用DEAE Sephadex A-50凝胶吸附法从去冷沉淀血浆上清液（cryoprecipitate reduced plasma supernatant，CRPS）分离纯化人凝血酶原复合物（human prothrombin complex concentrate， PCC）的可行性。方法采用凝胶吸附法从CRPS中连续制备3批次PCC制品，对该工艺中PCC原液、半成品和成品的人凝血因子Ⅸ（human coagulation factor Ⅸ, FⅨ）效价回收率、杂蛋白含量、干热病毒灭活效果进行检测分析；对PCC成品进行检定分析和稳定性试验。结果以CRPS中FⅨ效价为100%，凝胶吸附工艺中PCC原液、半成品、成品的FⅨ效价回收率分别为（65.0±2.1）%、（56.3±4.2）%、（40.3±1.8）%；原液中杂蛋白含量较低；干热处理前后各项质量指标均合格。PCC成品检定显示，其物理、化学、效价与FⅨ比活性、活化凝血因子活性等质量指标均满足中国药典2020年版三部要求。加速和长期稳定性试验的各项质量指标检测结果与0个月相比虽有所浮动，但均合格。结论采用DEAE Sephadex A-50凝胶吸附法可成功从CRPS中分离纯化出PCC。正文人凝血酶原复合物（human prothrombin complex concentrate，PCC）是由维生素K介导、在肝脏内合成的糖蛋白。PCC制剂主要由人凝血因子（human coagulation factor ，F）Ⅱ、FⅦ、FⅨ和FⅩ 4种凝血因子组成，临床上常被用于乙型血友病、肝功能损伤等凝血功能障碍疾病的辅助治疗。 DEAE Sephadex A-50凝胶为弱碱性阴离子交换剂，在pH7.2~7.4的环境中能吸附大部分酸性蛋白，且该凝胶的蛋白结合能力强、稳定性好。本研究拟用该凝胶吸附方法分离纯化去冷沉淀血浆上清液（cryoprecipitate reduced plasma supernatant，CRPS）中的PCC，根据中国药典2020年版三部（药典三部）的要求检测相关质量指标，并对成品进行加速和长期稳定性试验，考察各项质量指标的变化情况，为PCC储存环境和有效期的研究提供依据。 1 材料与方法 1.1 样品 3批次CRPS（批号：1、2、3）均由国药集团上海血液制品有限公司制备并提供。 1.2 主要试剂与仪器氯化钠购自江苏省勤奋药业有限公司；枸橼酸钠购自湖南尔康制药股份有限公司；吐温80购自德国Merck公司；磷酸三丁酯（tri-n-butyl phosphate，TNBP）、盐酸、醋酸和氢氧化钠均购自国药集团化学试剂有限公司；醋酸钠购自上海试四赫维化工有限公司；氨基酸购自上海味之素氨基酸有限公司；DEAE SephadexTM A-50型凝胶购自美国GE公司；GB150-1998型吸附罐A和吸附罐B均购自上海日泰医药设备工程有限公司；Pellicon-2型超滤系统购自美国Millipore公司；ACL TOP-300型全自动凝血仪购自美国沃芬公司。 1.3 PCC的制备 1.3.1　凝胶吸附　按照质量比1 000∶3将每批次CRPS和凝胶干粉加入吸附罐A中，搅拌吸附后排出滤液。然后用洗涤液（10 mmol/L枸橼酸钠溶液和100 mmol/L氯化钠溶液）反复洗涤吸附后的凝胶以去除杂蛋白，再使用解离液（10 mmol/L 枸橼酸钠和1 000 mmol/L氯化钠）将目标蛋白与凝胶分离。目标蛋白溶液经超滤脱盐得PCC，再加入有机溶剂/去污剂混合物灭活剂（质量分数50% 吐温80和15% TNBP），24~26 ℃灭活6 h。将灭活处理后的PCC转移至吸附罐B中，按照1 000 g CRPS 加入1 g凝胶干粉的比例，搅拌吸附后排出滤液，然后用洗涤液去除杂蛋白和残留的灭活剂，用解离液处理获取目标蛋白。 1.3.2　成品制备　对目标蛋白进行第2次超滤脱盐，得PCC原液。收集超滤滤液，加入氨基酸将pH调至7.0，即得PCC半成品。再将其除菌分装至模制瓶中，经冻干后置于80 ℃恒温箱中持续保温72 h进行干热病毒灭活，即得PCC成品。 1.4 凝胶吸附工艺检测 1.4.1　FⅨ效价回收率检测　采用药典三部通则3519的一期法测定凝胶吸附试验中CRPS、PCC原液、PCC半成品、PCC成品的FⅨ效价，以CRPS中FⅨ效价为100.0%，根据下列公式计算3批次中各级FⅨ效价回收率，并计算其均值。 1.4.2　杂蛋白含量检测　采用免疫散射浊度法对3批PCC原液中的IgG、IgA、IgM、人血白蛋白（human albumin，ALB）和纤维连接蛋白（fibronectin，Fn）等杂蛋白含量进行检测。 1.4.3　干热病毒灭活效果　采用1.4.1的方法分别测定3批次干热灭活处理前的PCC冻干品和经80 ℃干热灭活处理72 h后的PCC成品的FⅨ效价，干热灭活处理后FⅨ效价应为8.0~14.0 国际单位（international unit，IU）/mL；采用药典三部通则0731的第一法检测二者中的蛋白质含量，并计算其对应的FⅨ比活性，即FⅨ效价与蛋白质含量的比值，FⅨ比活性应不低于0.5 IU/mg蛋白质；肉眼观察二者的外观，加入20~30 ℃灭菌注射用水，轻轻摇动复溶后再次进行观察，干热灭活处理前后制品的外观均应为白色或灰绿色疏松体，加入20~30 ℃灭菌注射用水复溶后，均应为无色、淡黄色、淡蓝色或黄绿色澄明液体，可带轻微乳光；检测二者加入20~30 ℃灭菌注射用水的复溶时间，应在15 min内完全溶解；采用灯检法检查二者的可见异物指标，不得检出金属屑、玻璃屑、长度＞2 mm的纤维、最大粒径＞2 mm的块状物以及静置一定时间后轻轻旋转时肉眼可见的烟雾状微粒沉积物、无法计数的微粒群或摇不散的沉淀，以及在规定时间内较难计数的蛋白质絮状物等明显可见异物。 1.5 PCC成品检定 1.5.1　物理检测　3批PCC成品的外观、复溶时间和可见异物指标检测及可接受标准参照1.4.3，渗透压摩尔浓度采用药典三部通则0632的冰点下降法检测，可接受标准：渗透压摩尔浓度为240～450 mOsmol/kg。 1.5.2　化学检测　按照药典三部的要求，采用通则0832库伦滴定法检测PCC成品的水分含量，应≤3.0%；采用通则0631电位法检测PCC成品pH值，应为6.5～7.5；采用通则3110火焰光度法检测PCC成品钠离子含量，应≤160 mmol/L；采用通则3108高效液相色谱法检测PCC成品枸橼酸离子含量，应≤25 mmol/L；采用通则3205气相色谱法检测PCC成品TNBP残留量，应≤10 μg/mL；采用通则3203比色法检测吐温80残留量，应≤100 μg/mL；采用通则3123高效液相色谱法检测氨基酸含量，应为0.10~0.30 mol/L。 1.5.3　效价和比活性检测　按1.4.1方法测定3批次PCC成品的FⅨ效价，并按照1.4.3的方法计算FⅨ比活性，要求FⅡ效价≥8.0 IU/mL，FⅦ效价≥5.3 IU/mL，FⅨ效价在8.0~14.0 IU/mL，FⅩ效价≥8.0 IU/mL。 1.5.4　其他项目检测　根据药典三部要求检测PCC成品的人凝血酶活性、凝血因子活性、无菌性、异常毒性、热原、HBV表面抗原（hepatitis B surface antigen， HBsAg）。将3批PCC成品分别和人纤维蛋白原充分混合后，肉眼观察判断其人凝血酶活性， PCC成品应无凝块或纤维蛋白析出；向PCC成品加适量pH 7.5的三羟甲基氨基甲烷缓冲液，至FⅨ效价为 20 IU/mL，并检定其活化的凝血因子活性，供试品稀释液凝固时间均应≥150 s；采用薄膜过滤法对PCC成品进行无菌检查，供试品管应澄清，或虽显浑浊但经确证无菌生长；采用小鼠试验法进行异常毒性检查，7 d观察期内，小鼠应全部健存，且无异常反应，7 d后每只小鼠体重应增加；采用家兔法进行热原检查， 3只家兔注射供试品后的体温变化均＜0.6 ℃且升温总和＜1.3 ℃为合格；采用ELISA检测HBsAg，应为阴性。 1.5.5　稳定性试验 1.5.5.1　加速稳定性试验　将3批PCC成品于（25±2） ℃、相对湿度（60±10）%的条件下放置6个月，第0、3和6个月月末分别取样，采用药典三部通则3519的一期法检测样品FⅡ、FⅦ、FⅨ和FⅩ效价，检测方法及结果标准参照1.4.3和1.5.3。 1.5.5.2　长期稳定性试验　将3批PCC成品存放于（5±3） ℃、相对湿度（60±10）%条件下24个月，第0、12和24个月月末分别取样，按1.5.5.1方法检测样品FⅡ、FⅦ、FⅨ和FⅩ效价，检测方法及结果标准参照1.4.3和1.5.3。 1.6 统计学分析使用Excel 2020软件对实验数据进行统计分析，数据用均值±标准差表示。组间比较采用单因素方差分析，P＞0.05表示差异无统计学意义。 2 结果 2.1 FⅨ效价回收率各工艺阶段FⅨ效价回收率呈递减趋势，以CRPS的FⅨ效价为100%，PCC原液、PCC半成品和PCC成品回收率分别为（65.0±2.1）%、（56.3±4.2）%和（40.3±1.8）%，见图1。这表明凝胶吸附过程中超滤截留、凝胶吸附、干热处理等操作对FⅨ效价均会造成一定损失。 2.2 杂蛋白含量对PCC原液样品进行杂蛋白检测分析，结果如表1所示，IgG、IgA、IgM、ALB和Fn含量分别为≤0.6 、≤0.5 、＜0.2 、＜0.4 和≤0.2 g/L。各种杂蛋白残留量均保持较低的水平，表明2次凝胶吸附和超滤操作能够去除PCC中的大部分杂蛋白，降低了蛋白质含量，从而获得较高比活性的制品。 2.3 干热病毒灭活效果各指标的检测结果见表2。3批次干热处理后PCC成品的FⅨ效价均在8.0~14.0 IU/mL之间，FⅨ比活性均不低于0.5 IU/mg蛋白质，且二者干热处理前后的检测值间的差异不具有统计学意义，F值分别为6.63、1.80，P值均＞0.05。干热处理前后制品的外观均为白色疏松体，复溶时间均小于10 min，可见异物检查正常，均未出现金属屑、玻璃屑、长度超过2 mm的纤维、以及白色絮状物或颗粒等现象。表明干热处理对PCC制品的质量影响不显著。 2.4 PCC成品检定 2.4.1　物理检测结果　物理检测实验结果显示，3批PCC成品的外观成型均较好，为白色疏松体；复溶时间均在10 min以内，复溶后均为淡蓝色溶液且乳光较轻；可见异物检测中未发现絮状物或蛋白颗粒现象；渗透压摩尔浓度为（375.0±4.6） mOsmol/kg。 2.4.2　化学检测结果　对3批PCC成品进行化学检定，结果显示水分含量为（1.0±0.2）%、pH值为7.0±0.1、钠离子含量为（73.0±7.0） mmol/L、枸橼酸离子含量为（15.3±0.6） mmol/L、TNBP残留量为（0.3±0.4） μg/mL、吐温80残留量为（42.7±12.6） μg/mL、氨基酸含量为（0.2±0.0） mol/L。以上各指标的检定结果均符合药典三部标准，见表3。 2.4.3　效价与FⅨ比活性检测结果　对3批PCC成品的检测结果显示，FⅡ效价为（14.5±1.1） IU/mL，FⅦ效价为（10.8±1.2） IU/mL，FⅨ效价为（10.4±0.4） IU/mL，FⅩ效价为（13.9±0.4） IU/mL，FⅨ比活性计算结果为（0.7±0.1） IU/mg，见表4。各指标检测结果均符合药典三部的要求。 2.4.4　其他项目检测结果　3批PCC成品和人纤维蛋白原充分混合后均未观察到有凝块或纤维蛋白析出；活化凝血因子活性检查结果显示凝固时间为（394.9±18.6） s，均在150 s以上；无菌检查结果显示3批PCC成品的试管均澄清，无菌生长；异常毒性检查结果显示小鼠均无异常反应并健存，且体重增加；热原检查结果显示3只家兔升温值分别为（0.1±0.1） ℃、（0.2±0.1） ℃和（0.3±0.2） ℃，均＜0.6 ℃，且升温总和分别为（0.6±0.1） ℃、（0.6±0.2） ℃和（0.6±0.0） ℃，均＜1.3 ℃；ELISA显示，HBsAg结果均为阴性。 2.4.5　稳定性研究结果 2.4.5.1　加速稳定性试验结果各指标检测结果均合格。FⅡ、FⅦ、FⅨ和FⅩ效价指标检测结果如表5所示，与0个月相比虽有所浮动，但均合格。FⅡ效价均≥8.0 IU/mL，FⅦ效价均≥5.3 IU/mL，FⅨ效价均在8.0~14.0 IU/mL之间，FⅩ效价均≥8.0 IU/mL。对效价进行单因素方差分析，比较批次间的差异性，结果显示差异均无统计学意义（P值均＞0.05）。 2.4.5.2　长期稳定性试验结果 FⅡ、FⅦ、FⅨ和FⅩ效价指标检测结果如表6所示，与0个月相比虽有所浮动，但均合格。FⅡ效价均≥8.0 IU/mL，FⅦ效价均≥5.3 IU/mL，FⅨ效价均在8.0~14.0 IU/mL之间，FⅩ效价均≥8.0 IU/mL。对效价进行单因素方差分析，比较批次间的差异性，结果显示差异均无统计学意义（P值均＞0.05）。 3 讨论 PCC的制备技术主要包括无机盐吸附法和离子交换吸附法，采用无机盐吸附法制备的PCC虽能满足临床需求，但原料血浆中的枸橼酸盐或柠檬酸盐会干扰PCC的吸附，且被无机盐处理过的血浆难以制备ALB、人免疫球蛋白等其他产品，不利于血浆的综合利用。目前由新乡华兰生物工程股份有限公司、上海莱士血液制品股份有限公司等生产的市售PCC产品主要通过凝胶吸附法获得，其具体制备工艺以及PCC成品的FⅡ、FⅦ、FⅨ和FⅩ含量各不相同。本研究采用DEAE Sephadex A-50凝胶吸附法从CRPS中连续分离纯化并制备3批次PCC，在比较各阶段过程品的同时，根据药典三部要求对成品各项质量指标进行检测，并开展稳定性研究。首先分析了各工艺阶段的FⅨ效价回收率，结果表明，各级回收率均有损失，且逐级降低，可能原因为超滤过程存在的膜污染和浓差极化现象、除菌过滤过程中的高强度压差、以及冻干和干热处理等因素均会造成蛋白活性损失。然后对原液中的杂蛋白含量进行了检测与分析，发现凝胶吸附结合超滤工艺能实现较低的杂蛋白残留量。研究中还对干热处理前/后PCC制品的质量变化做了比较，结果发现FⅨ效价和比活性均有下降趋势。干热处理常用于凝血因子类产品的病毒灭活工艺，虽然已被证实可以灭活脂包膜和非脂包膜病毒，但对制品活性也会造成一定影响。对干热处理前/后FⅨ效价和比活性做单因素方差分析，结果表明差异不具有统计学意义。本研究还对PCC成品进行了检定分析，结果发现各项指标检测结果均满足药典三部规定，证明该工艺能去除绝大部分的化学物质残留，其中FⅨ的效价和比活性分别为（10.4±0.4） IU/mL和（0.7±0.1） IU/mg，与已有报道相仿。另外对各批次间FⅡ、FⅦ、FⅨ和FⅩ效价的差异性进行了统计学分析，结果表明均不具有统计学意义。综上所述，本研究采用DEAE Sephadex A-50凝胶吸附法从CRPS中成功制备出安全、稳定的PCC制品，为未来PCC的商业规模化生产奠定了基础。作者刘环1 张良1 曹璟1 杨帆1 方明阳2 江砚芳1 1国药集团上海血液制品有限公司血液制剂室，上海 200051；2国药集团昆明血液制品有限公司血液制剂室，昆明 650212 通信作者：江砚芳， Email：jiangyanfang@sinopharm.com 引用本文：刘环, 张良, 曹璟, 等. 人凝血酶原复合物的分离纯化工艺 [J]. 国际生物制品学杂志, 2025, 48(4): 241-246. DOI: 10.3760/cma.j.cn311962-20241216-00088 识别微信二维码，添加生物制品圈小编，符合条件者即可加入生物制品微信群！请注明：姓名+研究方向！版权声明本公众号所有转载文章系出于传递更多信息之目的，且明确注明来源和作者，不希望被转载的媒体或个人可与我们联系(cbplib@163.com)，我们将立即进行删除处理。所有文章仅代表作者观不本站。

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2025-07-15

·FiercePharma

PCI, on CDMO growth journey, nets 'sizable' investment from private equity heavyweights

PCI did not disclose financial terms of the private transaction, though a media relations representative for the company described the investment round as “both sizable and significant.” With transatlantic expansions nearing completion and a new acquisition in the books, PCI Pharma Services has secured a confidence vote—and capital to go with it—from a slate of private equity heavy hitters.The Philadelphia-based CDMO has received a new strategic investment co-led by Bain Capital and the company’s resident lead investor Kohlberg, PCI said in a July 14 press release. Mubadala Investment Company also chipped in a “significant reinvestment,” while Partners Group will “continue to support the company with a minority investment," according to the release.PCI did not disclose the financial terms of the private transaction, though a media relations representative for the company described the investment round as “both sizable and significant.”The deal values PCI at $10 billion, The Wall Street Journal reported Monday, citing people close to the matter.While Bain is new to the mix, Kohlberg and Mubadala first invested in PCI back in 2020.Together, the three private equity firms are now partnering with PCI’s management to accelerate growth, build on the company’s customer service acumen and help more PCI clients get innovative biologics to market, according to the CDMO’s release.PCI says it will use the extra cash to pursue both internal and external projects, including growing its CDMO services suite and its geographic footprint. Looking ahead, the company aims to expand its existing injectable fill-finish capabilities, as well as those for high-potency and specialized manufacturing. In September, the CDMO unveiled a $365 million investment to bulk up in assembly and packaging of drug-device products, both at home and abroad.Aside from upgrades to existing sites in Pennsylvania and Illinois, the 2024 outlay also went toward the purchase of a packaging and assembly plant near Dublin and an expansion at the company’s existing CityNorth Dublin Campus in Ireland.At the time, PCI said it expected the expansions at its site in Rockford, Illinois, and the CityNorth campus in Ireland to be up and running by 2025’s third quarter. More recently, PCI acquired a 100% stake in Ajinomoto’s fill-finish contracting arm Ajinomoto Althea. The deal, for which financial terms weren’t disclosed, netted PCI its first production site in North America for prefilled syringes and cartridges, the CDMO said in late April.Outside the U.S., PCI boasts manufacturing operations in Australia, Canada, the U.K. and Europe.

并购引进/卖出

2025-06-04

·PRNewswire

Ajinomoto Health & Nutrition North America, Inc. Opens Quality Control Laboratory Following $2.1M Renovation

RALEIGH, N.C., June 4, 2025 /PRNewswire/ -- Ajinomoto Health & Nutrition North America, Inc. (AHN), a global leader in amino acid manufacturing, celebrated the opening of its renovated Quality Control Laboratory today with a ribbon-cutting ceremony. Global senior leaders and dedicated team members who have been integral to the renovation efforts gathered at the modern facility on AHN's Raleigh, North Carolina, campus. The re-envisioned lab showcases AHN's commitment to delivering top product quality and leading safety standards. "By updating our facilities, we are even more equipped to meet the evolving needs of our customers and maintain our position as a leader in the industry," said Jessica Lee, Quality Manager. "Our Quality Control Laboratory is part of Ajinomoto Health and Nutrition's ongoing investment in quality and innovation." With the expanding need for amino acids in today's market, AHN's Quality Control Laboratory features advanced analytical equipment, improved workflow efficiencies, and enhanced safety measures. The facility benefits from Raleigh's skilled workforce, top universities, and numerous life sciences support companies, strengthening the area's reputation as a leading biotech hub. The enhancements also support AHN's growth plan for supplying Active Pharmaceutical Ingredient (API) amino acids and blends globally. By investing in these upgrades, AHN is positioning itself to meet the increasing global demand for high-quality APIs. The improved laboratory enables AHN to scale production and maintain stringent quality standards across larger volumes. This strategic investment aligns with AHN's long-term vision of expanding its market presence and reinforcing its reputation as a reliable supplier in the pharmaceutical industry. "The strategic investments made by AHN underscore our dedication to 'AminoScience,' the Ajinomoto Group's unique scientific approach to maximizing resources, resolving social issues, and contributing to people's wellbeing," says Ajinomoto Health & Nutrition's President and CEO, Ikuo Kira. The Ajinomoto Group connects its global divisions to deliver high-quality health and nutrition solutions by integrating research-based functions, technologies, and services centered on amino acids. About Ajinomoto Health & Nutrition North America, Inc. Ajinomoto Health & Nutrition North America, Inc. is a wholly-owned subsidiary of the Ajinomoto Group, a global leader in the research, development, manufacture, and sale of amino acid-based products for the pharmaceutical, nutraceutical, sports nutrition, health and beauty industries, as well as food ingredients. The company opened its first U.S. office in New York in 1917 and has since grown and expanded its presence, establishing offices and production facilities in North Carolina, Iowa, Ohio, Massachusetts, and Illinois. Ajinomoto Health & Nutrition North America, Inc. leverages an international manufacturing, supply, and distribution chain to bring the highest-grade products to customers. For additional information on Ajinomoto Health & Nutrition North America, Inc., please visit . Media contact: Charlotte Eby (515) 577-3171, [email protected] SOURCE Ajinomoto Health & Nutrition North America, Inc WANT YOUR COMPANY'S NEWS FEATURED ON PRNEWSWIRE.COM? 440k+ Newsrooms & Influencers 9k+ Digital Media Outlets 270k+ Journalists Opted In GET STARTED

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