http://www.ubiasia.com.tw/News/Default.asp?SN=135
造兩線 (可擴成四線) 2,000公升級的單株抗體藥品製造廠
-->單株抗體藥品商品化 UB-421抗體目前已順利推展至臨床二期，
聯亞切割單株抗體藥品事業部切割 2013 10 + 台塑生醫 8億(25%持股) 設廠虎口 竹北生醫園區
聯生藥 董事長 王長怡
台灣為研發基地、大中華為市場腹地、以UBI為樞紐進入全球市場的集團佈局
台塑生醫王瑞瑜董事長
以UBI集團在生物醫學領域深厚的研發技術基礎以及台塑生醫與台塑集團醫院體系在醫療運用及臨床上的豐富經驗，可獲致藥品產業最完整的綜效。
聯亞還擁有多項其他類別產品線包括系列新代蛋白質藥物、具預防性與治療用之創新設計型疫苗、可應用於骨材/牙根植體的骨質生長因子BMP-2，以及通過美國FDA GMP認證的無菌針劑生產線
聯亞生技執行副總林淑菁博士
14年來，經由發展愛滋病治療性單株抗體UB-421，由抗體擬人化、實驗室製程開發、分析方法建立、工業製程建立、GMP 先導工廠建立、前臨床靈長動物試驗到人體臨床試驗等過程
主要幹部年齡平均不到40歲卻共事超過10年以上，透過集體學習、高度工作熱誠以及團隊合作，不但創造了高價值的技術與產品，更造就了個人的專業與企業價值。
聯亞仍將繼續推動阿茲海默症疫苗與系列產品線、動物保健產品事業、非抗體蛋白質藥品之事業分割計劃，
台灣從『販賣知識產權』之生技新藥產業發展思維轉換提升為建立擁有知識產權創新產品與製造能力的正確模式，以真正開創繼半導體與電子產業後的另一個支柱型產業。
3/23/2015
聯生藥投資12億 湖口建蛋白質藥廠
http://www.appledaily.com.tw/appledaily/article/finance/20150209/36378238/
2015/2/9
新竹湖口工業區「研發暨蛋白質藥廠綜合大樓」
台灣首次由抗體藥廠率先建構的原料(CMO)廠。
聯生藥近期將接受台美工業合作技轉計劃訓練，加上美生技工程巨擘奇異(GE)將來台，接受聯生藥蛋白質藥產程優化、放大等技術轉移，創下台灣工業合作領域生技技轉首例。
2015/2/9
新竹湖口工業區「研發暨蛋白質藥廠綜合大樓」
台灣首次由抗體藥廠率先建構的原料(CMO)廠。
聯生藥近期將接受台美工業合作技轉計劃訓練，加上美生技工程巨擘奇異(GE)將來台，接受聯生藥蛋白質藥產程優化、放大等技術轉移，創下台灣工業合作領域生技技轉首例。
蛋白藥有錢途 台廠爭相建廠
http://www.cpmda.org.tw/news_show_n1.php?news_id=1248
生技中心、永昕後，東洋(東洋董事長林榮錦) 和台灣醣聯(與日本合作 董事長張東玄)
全球哺乳動物細胞生產單株抗體技術的蛋白藥Amgen、Genentech、Biogen Idec
英國的Lonza 德國的Boehringer Ingelheim 代工
日本TBI 半代工 4000L
台灣: 生技中心 永昕
CMO產能的數量 兩萬升 以下只能提供給CRO公司臨床實驗用
2014年學名專利藥到期,欣欣蛋白質藥每年產值10億美元
生技中心、永昕後，東洋(東洋董事長林榮錦) 和台灣醣聯(與日本合作 董事長張東玄)
全球哺乳動物細胞生產單株抗體技術的蛋白藥Amgen、Genentech、Biogen Idec
英國的Lonza 德國的Boehringer Ingelheim 代工
日本TBI 半代工 4000L
台灣: 生技中心 永昕
CMO產能的數量 兩萬升 以下只能提供給CRO公司臨床實驗用
2014年學名專利藥到期,欣欣蛋白質藥每年產值10億美元
3/10/2008
The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle
source: BMC Structural Biology 2007, 7:34
The NMR structure of the murine DLC2 SAM domain reveals a
variant fold that is similar to a four-helix bundle
Jamie J Kwan and Logan W Donaldson*
Address: Department of Biology, York University, 4700 Keele Street, Toronto, Ontario M3J 1P3, Canada
Email: Jamie J Kwan - jkwan@yorku.ca; Logan W Donaldson* - logand@yorku.ca
* Corresponding author
Abstract
Background:
The tumor suppressor DLC2 (Deleted in Liver Cancer -2) participates in cell
signaling at the mitochondrial membrane. DLC2 is characterized by a SAM (sterile alpha motif)
domain, a Rho GTPase activating protein (GAP) domain, and a START lipid transfer domain.
Results:
Towards understanding the function of DLC2, we have solved the NMR solution
structure of the SAM domain. The DLC2-SAM domain structure reveals an atypical four-helix
composition that is distinct from the five-helix SAM domain structures that have been determined
to date. From structural alignments, helix 3 of the canonical SAM domain appears to be replaced
by shorter, extended secondary structure that follows a similar path. Another difference is
demonstrated by helices 1 and 2 that form a helical hairpin that is situated approximately parallel
to the canonical helix 5.
Conclusion:
The DLC2-SAM domain adopts a structure that is topologically more similar to an
anti-parallel four-helix bundle than a canonical SAM domain. This alternate topology may allow the
DLC2-SAM domain to interact with a novel set of ligands.
The NMR structure of the murine DLC2 SAM domain reveals a
variant fold that is similar to a four-helix bundle
Jamie J Kwan and Logan W Donaldson*
Address: Department of Biology, York University, 4700 Keele Street, Toronto, Ontario M3J 1P3, Canada
Email: Jamie J Kwan - jkwan@yorku.ca; Logan W Donaldson* - logand@yorku.ca
* Corresponding author
Abstract
Background:
The tumor suppressor DLC2 (Deleted in Liver Cancer -2) participates in cell
signaling at the mitochondrial membrane. DLC2 is characterized by a SAM (sterile alpha motif)
domain, a Rho GTPase activating protein (GAP) domain, and a START lipid transfer domain.
Results:
Towards understanding the function of DLC2, we have solved the NMR solution
structure of the SAM domain. The DLC2-SAM domain structure reveals an atypical four-helix
composition that is distinct from the five-helix SAM domain structures that have been determined
to date. From structural alignments, helix 3 of the canonical SAM domain appears to be replaced
by shorter, extended secondary structure that follows a similar path. Another difference is
demonstrated by helices 1 and 2 that form a helical hairpin that is situated approximately parallel
to the canonical helix 5.
Conclusion:
The DLC2-SAM domain adopts a structure that is topologically more similar to an
anti-parallel four-helix bundle than a canonical SAM domain. This alternate topology may allow the
DLC2-SAM domain to interact with a novel set of ligands.
10/23/2007
Conformational stability and DNA binding energetics of the rat thyroid transcription factor 1 homeodomain
Research Article
Conformational stability and DNA binding energetics of the rat thyroid transcription factor 1 homeodomain Pompea Del Vecchio 1 *, Paola Carullo 1, Guido Barone 1, Bruno Pagano 2, Giuseppe Graziano 3, Alessio Iannetti 4, Renato Acquaviva 4, Antonio Leonardi 4, Silvestro Formisano 4
1Dipartimento di Chimica, Università di Napoli Federico II, Via Cintia, 80126, Napoli, Italy
2Dipartimento di Scienze Farmaceutiche, Università di Salerno, Via Ponte Don Melillo, 84084 Fisciano (SA), Italy
3Dipartimento di Scienze Biologiche ed Ambientali, Università del Sannio, Via Port'Arsa 11, 82100 Benevento, Italy
4Dipartimento di Biologia e Patologia Cellulare e Molecolare L. Califano, Università di Napoli Federico II, Via Pansini, 5, 80131 Napoli, Italy
Abstract
The conformational stability of the rat thyroid transcription factor 1 homeodomain, TTF-1HD, has been investigated by means of circular dichroism (CD) and differential scanning calorimetry (DSC) measurements at pH 5.0 as a function of KCl concentration. Thermal unfolding of TTF-1HD is a reversible two-state transition. The protein is not stable against temperature, showing a denaturation temperature of 32蚓 in the absence of salt and 50蚓 at 75 mM KCl. The binding energetics of TTF-1HD to its target DNA sequence has been characterized by means of isothermal titration calorimetry (ITC) measurements, complemented with CD data. At 25蚓, pH 5.0 and 75 mM KCl, the binding constant amounts to 1.5 ?108M-1 and the binding enthalpy change amounts to -41 kJ mol-1. The process is enthalpy driven, but also the entropy change is favorable to complex formation. To gain a molecular level understanding of the interactions determining the association of TTF-1HD to the target DNA sequence structural information would be requested, but it is not yet available. Therefore, structural models of two complexes, TTF-1HD with the target DNA sequence and TTF-1HD with a modified DNA sequence, have been constructed by using as a template the NMR structure of the complex between NK-2 HD and its target DNA, and by performing molecular dynamics simulations 3.5 ns long. Analysis of these models allows one to shed light on the origin of the DNA binding specificity characteristic of TTF-1HD. Proteins 2007. © 2007 Wiley-Liss, Inc.
--------------------------------------------------------------------------------
Received: 10 October 2006; Revised: 12 March 2007; Accepted: 22 March 2007
Digital Object Identifier (DOI)
10.1002/prot.21552 About DOI
Conformational stability and DNA binding energetics of the rat thyroid transcription factor 1 homeodomain Pompea Del Vecchio 1 *, Paola Carullo 1, Guido Barone 1, Bruno Pagano 2, Giuseppe Graziano 3, Alessio Iannetti 4, Renato Acquaviva 4, Antonio Leonardi 4, Silvestro Formisano 4
1Dipartimento di Chimica, Università di Napoli Federico II, Via Cintia, 80126, Napoli, Italy
2Dipartimento di Scienze Farmaceutiche, Università di Salerno, Via Ponte Don Melillo, 84084 Fisciano (SA), Italy
3Dipartimento di Scienze Biologiche ed Ambientali, Università del Sannio, Via Port'Arsa 11, 82100 Benevento, Italy
4Dipartimento di Biologia e Patologia Cellulare e Molecolare L. Califano, Università di Napoli Federico II, Via Pansini, 5, 80131 Napoli, Italy
Abstract
The conformational stability of the rat thyroid transcription factor 1 homeodomain, TTF-1HD, has been investigated by means of circular dichroism (CD) and differential scanning calorimetry (DSC) measurements at pH 5.0 as a function of KCl concentration. Thermal unfolding of TTF-1HD is a reversible two-state transition. The protein is not stable against temperature, showing a denaturation temperature of 32蚓 in the absence of salt and 50蚓 at 75 mM KCl. The binding energetics of TTF-1HD to its target DNA sequence has been characterized by means of isothermal titration calorimetry (ITC) measurements, complemented with CD data. At 25蚓, pH 5.0 and 75 mM KCl, the binding constant amounts to 1.5 ?108M-1 and the binding enthalpy change amounts to -41 kJ mol-1. The process is enthalpy driven, but also the entropy change is favorable to complex formation. To gain a molecular level understanding of the interactions determining the association of TTF-1HD to the target DNA sequence structural information would be requested, but it is not yet available. Therefore, structural models of two complexes, TTF-1HD with the target DNA sequence and TTF-1HD with a modified DNA sequence, have been constructed by using as a template the NMR structure of the complex between NK-2 HD and its target DNA, and by performing molecular dynamics simulations 3.5 ns long. Analysis of these models allows one to shed light on the origin of the DNA binding specificity characteristic of TTF-1HD. Proteins 2007. © 2007 Wiley-Liss, Inc.
--------------------------------------------------------------------------------
Received: 10 October 2006; Revised: 12 March 2007; Accepted: 22 March 2007
Digital Object Identifier (DOI)
10.1002/prot.21552 About DOI
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