JP2007508011A - ヒトヒンジコアミメティボディ、組成物、方法および用途 - Google Patents
ヒトヒンジコアミメティボディ、組成物、方法および用途 Download PDFInfo
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- JP2007508011A JP2007508011A JP2006534031A JP2006534031A JP2007508011A JP 2007508011 A JP2007508011 A JP 2007508011A JP 2006534031 A JP2006534031 A JP 2006534031A JP 2006534031 A JP2006534031 A JP 2006534031A JP 2007508011 A JP2007508011 A JP 2007508011A
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Abstract
Description
本発明は、当該技術分野において既知であるものと組み合わせて、本明細書において記述されそして/もしくは可能にされるような、改変された免疫グロブリン、切断生成物ならびにその他の特定の部分およびバリアントを包含する、単離されたヒトヒンジコアミメティボディ、ならびにヒンジコアミメティボディ組成物、コードもしくは相補的核酸、ベクター、宿主細胞、組成物、製剤、装置、トランスジェニック動物、トランスジェニック植物、ならびにその製造および使用方法を提供する。
((V(m)−P(n)−L(o)−H(p)−CH2(q)−CH3(r))(s)
[式中、Vは免疫グロブリン可変領域のN末端の少なくとも1つの部分であり、Pは少なくとも1つの生物活性ペプチドであり、Lは少なくとも一つのリンカーポリペプチドであり、Hは少なくとも一つの免疫グロブリンヒンジ領域の少なくとも1つの部分であり、CH2は免疫グロブリンCH2定常領域の少なくとも1つの部分であり、CH3は免疫グロブリンCH3定常領域の少なくとも1つの部分であり、m、n、o、p、q、rおよびsは独立して0、1もしくは2〜10の間の整数である]
を含んでなる。
アントをコードするポリヌクレオチドを含んでなるか、それに相補的であるか、それに有意な同一性を有するかもしくはハイブリダイズする単離された核酸分子を提供する。本発明はさらに、該単離されたヒンジコアミメティボディ核酸分子の少なくとも1つを含んでなる組み換えベクター、そのような核酸および/もしくは組み換えベクターを含有する宿主細胞、ならびにそのようなヒンジコアミメティボディ核酸、ベクターおよび/もしくは宿主細胞を製造しそして/もしくは使用する方法を提供する。
組成物は、場合により少なくとも1つの追加化合物、タンパク質もしくは組成物をさらに含んでなることができる。
非経口、皮下、筋肉内、静脈内、関節内、気管支内、腹内、嚢内、軟骨内、腔内(intracavitary)、腔内(intracelial)、小脳内、脳室内、結腸内、頸内、胃内、肝臓内、心筋内、骨内、骨盤内、心膜内、腹腔内、胸膜腔内、前立腺内、肺内、直腸内、腎臓内、網膜内、脊椎内、滑液包内、胸内、子宮内、膀胱内、ボーラス、膣、直腸、口腔、舌下、鼻腔内もしくは経皮送達装置もしくは系の成分として該容器を有することを含んでなることができる。
本発明は、単離された、組み換えおよび/もしくは合成のミメティボディまたは特定の部分もしくはバリアント、ならびに組成物および少なくとも1つのヒンジコアミメティボディをコードする少なくとも1つのポリヌクレオチドを含んでなるコード核酸分子を提供する。本発明のそのようなミメティボディまたは特定の部分もしくはバリアントは、特定のヒンジコアミメティボディ配列、ドメイン、フラグメントおよびその特定のバリアントを含んでなる。本発明はまた、治療組成物、方法および装置を包含する、該核酸およびミメティボディまたは特定の部分もしくはバリアントを製造しそして使用する方法も提供する。
((V(m)−P(n)−L(o)−H(p)−CH2(q)−CH3(r))(s)
[式中、Vは免疫グロブリン可変領域のN末端の少なくとも1つの部分であり、Pは少なくとも1つの生物活性ペプチドであり、Lはミメティボディが別の方向および結合特性を有することを可能にすることにより構造的柔軟性を与えるポリペプチドであり、Hは免
疫グロブリン可変ヒンジ領域の少なくとも1つの部分であり、CH2は免疫グロブリンCH2定常領域の少なくとも1つの部分であり、CH3は免疫グロブリンCH3定常領域の少なくとも1つの部分であり、そしてm、n、o、p、q、rおよびsは独立して0、1もしくは2〜10の間の整数であることができる]
を含んでなる。m=1の場合のモノマーは、Cys−Cysジスルフィド結合もしくは他の免疫グロブリン配列のようなしかしこれらに限定されるものではない、会合もしくは共有結合により他のモノマーに連結されることができる。従って、本発明のヒンジコアミメティボディは、治療ペプチドおよびその生来のもしくは獲得したインビトロ、インビボもしくはin situ特性もしくは活性を提供しながら、その生来の特性および機能を有する抗体構造を模倣する。本発明の少なくとも1つのヒンジコアミメティボディの抗体の様々な部分および治療ペプチド部分は、当該技術分野において既知であるものと組み合わせて本明細書に記述されるように異なることができる。
本発明の単離された核酸は、少なくとも1つのヒンジコアミメティボディ、フラグメントもしくはその特定のバリアントの製造に用いることができ、それは細胞、組織、臓器もしくは動物(哺乳類およびヒトを包含する)において、免疫障害もしくは疾患、心臓血管障害もしくは疾患、感染性、悪性および/もしくは神経障害もしくは疾患、貧血;免疫/自己免疫;ならびに/または癌性/感染性ならびに他の既知のもしくは特定のタンパク質
関連症状の少なくとも1つから選択されるがこれらに限定されるものではない、少なくとも1つのタンパク質関連症状を調節するか、処置するか、緩和するか、その発生を防ぐのに役立つか、もしくはその症状を減らすことをもたらすために用いることができる。
本明細書に引用する全ての公開もしくは特許は、それらが本発明の時点での最新技術を示すようにそして/もしくは本発明の説明および実施可能性を提供するために引用することにより本明細書に全部が組み込まれる。公開は、任意の科学的もしくは特許公開、または全ての記録、電子もしくは印刷形式を包含する任意のメディア形式で利用可能な任意の他の情報をさす。以下の参考文献は、引用することにより本明細書に全部が組み込まれる:Ausubel,et al.,ed.,Current Protocols in Molecular Biology,John Wiley & Sons,Inc.,NY,NY(1987−2003);Sambrook,et al.,Molecular Cloning:A Laboratory Manual,2nd Edition,Cold Spring Harbor,NY(1989);Harlow and Lane,Antibodies,a Laboratory Manual,Cold Spring Harbor,NY(1989);Colligan,et al.,eds.,Current Protocols in Immunology,John Wiley & Sons,Inc.,NY(1994−2003);Colligan et al.,Current Protocols in Protein Science,John Wiley & Sons,NY,NY,(1997−2003)。
ヒンジコアミメティボディは、場合により少なくとも1つの可変抗体配列の少なくとも一部(V)とさらに直接連結している、少なくとも1つの治療ペプチド(P)に直接連結している、任意のリンカー配列(L)と直接連結している、少なくとも1つのコアヒンジ領域を含んでなるような、少なくとも1つのヒンジ領域フラグメントの少なくとも一部(H)と直接連結している少なくとも1つのCH2領域と直接連結している少なくとも1つのCH3領域を場合により含んでなることができる。1対のCH3−CH2−H−L−Vの好ましい態様として、該対は会合もしくは共有結合により連結されることができる。従って、本発明のヒンジコアミメティボディは、治療ペプチドおよびその生来のもしくは獲得したインビトロ、インビボもしくはin situ特性もしくは活性を提供しながら、その生来の特性および機能を有する抗体構造を模倣する。本発明の少なくとも1つのヒンジコアミメティボディの抗体の様々な部分および治療ペプチド部分は、当該技術分野において既知であるものと組み合わせて本明細書に記述されるように異なることができる。
:940−944(1994);およびその中に引用される参考文献も参照。上記の参考文献は、引用することにより本明細書に全部が組み込まれる。
その特定のフラグメント、バリアントもしくは共通配列をさらに含んでなる、配列番号:1〜979の少なくとも1つの連続するアミノ酸の少なくとも90〜100%をコードするヌクレオチド配列ならびに抗体の少なくとも1つの部分(ここで、上記の配列は、本発明のヒンジコアミメティボディを提供するために式(I)のP配列として挿入される)、またはこれらの配列の少なくとも1つを含んでなる寄託ベクターのような、本明細書に提供される情報を用いて、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントをコードする本発明の核酸分子を本明細書に記述されるかもしくは当該技術分野において既知であるような方法を用いて得ることができる。
を包含することができる。もちろん、遺伝暗号は当該技術分野において周知である。従って、本発明の特定のヒンジコアミメティボディまたは特定の部分もしくはバリアントをコードするそのような縮重核酸バリアントを作製することは当業者にとって日常的である。例えば、Ausubel,et al.,上記を参照、そしてそのような核酸バリアントは本発明に包含される。
本発明は、その特定のバリアントもしくは部分を包含する、本明細書に開示されるポリヌクレオチド、または本明細書に開示される他のものに選択的ハイブリダイゼーション条件下でハイブリダイズする単離された核酸を提供する。従って、この態様のポリヌクレオチドは、そのようなポリヌクレオチドを含んでなる核酸を単離すること、検出することおよび/もしくは定量することに用いることができる。
本発明の単離された核酸は、当該技術分野において周知であるように、(a)組み換え法、(b)合成技術、(c)精製技術、もしくはその組み合わせを用いて製造することができる。
例えば、ポリヌクレオチドの単離に役立つように1個もしくはそれ以上のエンドヌクレアーゼ制限部位を含んでなるマルチクローニング部位を核酸に挿入することができる。また、本発明の翻訳されたポリヌクレオチドの単離に役立つように翻訳可能な配列を挿入することができる。例えば、ヘキサヒスチジンマーカー配列は、本発明のタンパク質を精製するために都合のよい手段を提供する。本発明の核酸(コーディング配列を除く)は、場合により、本発明のポリヌクレオチドのクローニングおよび/もしくは発現用のベクター、アダプター、もしくはリンカーである。
RNA、cDNA、ゲノムDNA、もしくはその任意の組み合わせのような、本発明の単離された核酸組成物は、当業者に既知である任意の数のクローニング方法論を用いて生物学的供給源から得ることができる。ある態様として、適当なストリンジェンシー条件下で、本発明のポリヌクレオチドに選択的にハイブリダイズするオリゴヌクレオチドプローブが、cDNAもしくはゲノムDNAライブラリーにおける所望の配列を同定するために用いられる。RNAの単離、ならびにcDNAおよびゲノムライブラリーの構築は、当業者に周知である(例えば、Ausubel,上記;もしくはSambrook,上記を参照)。
本発明の単離された核酸はまた、既知の方法による直接化学合成により製造することもできる(例えば、Ausubel,et al.,上記を参照)。化学合成により一般的に一本鎖オリゴヌクレオチドが生成され、それを相補的配列とのハイブリダイゼーションにより、もしくは鋳型として該一本鎖を用いてDNAポリメラーゼでの重合により二本鎖DNAに転化することができる。DNAの化学合成は約100塩基もしくはそれ以上の配列に限定されることができるが、より長い配列は、より短い配列の連結により得られることができることを当業者は認識する。
本発明はさらに、本発明の核酸を含んでなる組み換え発現カセットを提供する。本発明の核酸配列、例えば、本発明のヒンジコアミメティボディまたは特定の部分もしくはバリアントをコードするcDNAもしくはゲノム配列は、少なくとも1つの所望の宿主細胞に導入することができる組み換え発現カセットを構築するために用いることができる。組み換え発現カセットは、典型的に、意図する宿主細胞におけるポリヌクレオチドの転写を導く転写開始調節配列に操作可能に連結された本発明のポリヌクレオチドを含んでなる。異種および非異種(すなわち、内因性)プロモーターの両方を本発明の核酸の発現を導くために用いることができる。
アンチセンスの方向のいずれかで発現することができる。センスもしくはアンチセンスの方向のいずれかにおける遺伝子発現の制御は、観察可能な特性に直接的な影響を有し得ることが理解される。抑制の別の方法は、センス抑制である。センスの方向に設定される核酸の導入は、それにより標的遺伝子の転写を阻止する有効な手段であることが示されている。
本発明はまた、当該技術分野において周知であるような、本発明の単離された核酸分子を含むベクター、組み換えベクターで遺伝子操作される宿主細胞、および組み換え技術による少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントの生産にも関する。例えば、各々引用することにより全部が本明細書に組み込まれる、Sambrook,et al.,上記;Ausubel,et al.,上記を参照。
定の部分もしくはバリアントのN末端に付加することができる。また、ペプチド部分も、精製を容易にするために本発明のヒンジコアミメティボディまたは特定の部分もしくはバリアントに付加することができる。そのような領域は、ヒンジコアミメティボディもしくはその少なくとも1つのフラグメントの最終調製の前に取り除くことができる。そのような方法は、Sambrook,上記、17.29〜17.42および18.1〜18.74章;Ausubel,上記、16、17および18章のような、多数の標準的な実験室マニュアルに記述されている。
ヒンジコアミメティボディまたは特定の部分もしくはバリアントは、プロテインA精製、硫酸アンモニウムもしくはエタノール沈殿、酸抽出、陰イオンもしくは陽イオン交換クロマトグラフィー、ホスホセルロースクロマトグラフィー、疎水性相互作用クロマトグラフィー、アフィニティークロマトグラフィー、ヒドロキシアパタイトクロマトグラフィーおよびレクチンクロマトグラフィーが包含されるがこれらに限定されるものではない周知の方法により組み換え細胞培養物から回収し、精製することができる。高速液体クロマトグラフィー(「HPLC」)もまた、精製に用いることができる。例えば、各々引用することにより全部が本明細書に組み込まれる、Colligan,Current Protocols in Immunology、もしくはCurrent Protocols in Protein Science,John Wiley & Sons,NY,NY,(1997−2001)、例えば、1、4、6、8、9、10章を参照。
本発明の単離されたミメティボディは、本明細書においてさらに完全に説明されるような本発明のポリヌクレオチドのいずれか1つによりコードされるヒンジコアミメティボディまたは特定の部分もしくはバリアント、あるいは任意の単離されたもしくは製造されたヒンジコアミメティボディまたはその特定の部分もしくはバリアントを含んでなる。
任意の数のペプチドを本発明とともに用いることができる。特に興味深いのは、EPO、TPO、成長ホルモン、G−CSF、GM−CSF、IL−1ra、レプチン、CTLA4、TRAIL、TGF−αおよびTGF−βの活性を模倣するペプチドである。ペプチドアンタゴニスト、特にTNF、レプチン、インターロイキン(IL−1〜IL−23など)のいずれか、および補体活性化に関与するタンパク質(例えばC3b)の活性に拮抗するものもまた興味深い。腫瘍ホーミングペプチド、膜輸送ペプチドなどを包含する、ターゲッティングペプチドもまた興味深い。ペプチドのこれらのクラスの全ては、本明細書に引用する参考文献および他の参考文献に記述されている方法により見出されることができる。
628:250−5(1991);Geissler K et al Recombinant human erythropoietin:A multipotential hemopoietic growth factor in vivo and in vitro.Contrib.Nephrol.87:1−10(1990);Gregory CJ Erythropoietin sensitivity as a differentiation marker in the hemopoietic system.Studies of three erythropoietic colony responses in culture.Journal of Cellular Physiology 89:289−301(1976);Jelkman W et al Monokines inhibiting erythropoietin production in human hepatoma cultures and in isolated perfused rat kidneys.Life Sci.50:301−8(1992);Kimata H et al Human recombinant erythropoietin directly stimulates B cell immunoglobulin production and proliferation in serum−free medium.Clinical and Experimental Immunology 85;151−6(1991);Kimata H et al Erythropoietin enhances immunoglobulin production and proliferation by human plasma cells in a serum−free medium.Clin.Immunology Immunopathol.59:495−501(1991);Kimata H et al Effect of recombinant human erythropoietin on human IgE production in vitro Clinical and Experimental Immunology 83:483−7(1991);Koury MJ and Bondurant MC Erythropoietin retards DNA breakdown and prevents programmed cell death in erythroid progenitor cells.Science 248:378−81(1990);Lim VS et al Effect of recombinant human erythropoietin on renal function in humans.Kidney International 37:131−6(1990);Mitjavila MT et al Autocrine stimulation by erythropoietin and autonomous growth of human erythroid leukemic cells in vitro.Journal of Clinical Investigation 88:789−97(1991);Andre M et al Performance of an immunoradiometric assay of erythropoietin and results for specimens from anemic and polycythemic patients.Clinical Chemistry 38:758−63(1992);Hankins WD et al Erythropoietin−dependent and erythropoietin−producing cell lines.Implications for research and for leukemia therapy.Annals of the New York Academy of Science 554:21−8(1989);Kendall RGT et al Storage and preparation of samples for erythropoietin radioimmunoassay.Clin.Lab.Haematology 13:189−96(1991);Krumvieh D et al Comparison of relevant biological assays for the determination of biological active erythropoietin.Dev.Biol.Stand.69:15−22(1988);Ma DD et al Assessment of an EIA for measuring human serum erythropoietin as compared with RIA and an in−vitro bioassay.British Journal of Haematology 80:431−6(1992);Noe G et al A sensitive sandwich ELISA for measuring erythropoietin in human serum British Journal of Haematology 80:285−92(1992);Pauly JU et al Highly specific and highly sensitive enzyme immunoassays for antibodies to human interleukin 3(IL3)and human erythropoietin(EPO)in serum.Behring Institut Mitteilungen 90:112−25(1991);Sakata S and Enoki Y Improved microbioassay for plasma erythropoietin based on CFU−E colony formation.Ann.Hematology 64:224−30(1992);Sanengen T et al Immunoreactive erythropoietin and erythropoiesis stimulating factor(s)in plasma from hypertransfused neonatal and adult mice.Studies with a radioimmunoassay and a cell culture assay for erythropoietin.Acta Physiol.Scand.135:11−6(1989);Widness JA et al A sensitive and specific erythropoietin immunoprecipitation assay:application to pharmacokinetic studies.Journal of Lab.Clin.Med.119:285−94(1992)を参照;さらなる情報についてはまた、個々のバイオアッセイにおいて使用される個々の細胞系も参照。上記の参考文献の各々は、引用することにより全部が本明細書に組み込まれる。EPOは、該因子に応答する、HCD57、NFS−60、TF−1およびUT−7のような細胞系を用いることによりアッセイすることができる。EPO活性はまた、骨髄細胞からCFU−Eの数を決定することによりコロニー形成アッセイにおいて評価することもできる。代わりのそして全く異なる検出方法は、サイトカインのRT−PCR定量である。
本発明のミメティボディまたは特定の部分もしくはバリアントを構成するアミノ酸は、略記されることが多い。アミノ酸表記は、以下の表22に提示するように、当該技術分野において汎用的であるような(Alberts,B.,et al.,Molecular Biology of The Cell,Third Ed.,Garland Publishing,Inc.,New York,1994を参照)その1文字コード、その3文字コード、名称、もしくは3ヌクレオチドコドン(1つもしくは複数)でアミノ酸を指定することにより表すことができる。
((V(m)−P(n)−L(o)−H(p)−CH2(q)−CH3(r))(s)
[式中、Vは免疫グロブリン可変領域のN末端の少なくとも1つの部分であり、Pは少なくとも1つの生物活性ペプチドであり、Lは少なくとも1つのリンカーポリペプチドであり、Hは少なくとも1つの免疫グロブリンヒンジ領域の少なくとも1つの部分であり、CH2は免疫グロブリンCH2定常領域の少なくとも1つの部分であり、CH3は免疫グロブリンCH3定常領域の少なくとも1つの部分であり、m、n、o、p、q、rおよびsは独立して0、1もしくは2〜10の間の整数である]
の使用に基づく。
nd Wells,Science 244:1081−1085(1989))のような、当該技術分野において既知である方法により同定することができる。後者の方法は、分子におけるあらゆる残基で単一のアラニン突然変異を導入する。次に、得られる突然変異体分子を、本明細書に特定されるようなもしくは当該技術分野において既知であるような、少なくとも1つのタンパク質関連活性のようなしかしこれに限定されるものではない、生物活性について試験する。ヒンジコアミメティボディまたは特定の部分もしくはバリアント結合にとって重要である部位はまた、結晶化、核磁気共鳴もしくは光親和性ラベリングのような構造解析により同定することもできる(Smith,et al.,J.Mol.Biol.224:899−904(1992)およびde Vos,et al.,Science 255:306−312(1992))。
活性のミメティボディまたは特定の部分もしくはバリアントは、天然の(非合成の)、内因性のもしくは関連するそして既知の挿入もしくは融合タンパク質または特定の部分もしくはバリアントのものの少なくとも20%、30%もしくは40%、そして好ましくは少なくとも50%、60%もしくは70%、そして最も好ましくは少なくとも80%、90%もしくは95%〜1000%の比活性を有する。酵素活性および基質特異性の大きさをアッセイしそして定量する方法は、当業者に周知である。
していることができ、または1つもしくはそれ以上の単位の不飽和を含有することができる。本発明のミメティボディを改変するために適当な脂肪酸には、例えば、n−ドデカノエート(C12、ラウレート)、n−テトラデカノエート(C14、ミリステート)、n−オクタデカノエート(C18、ステアレート)、n−エイコサノエート(C20、アラキデート)、n−ドコサノエート(C22、ベヘネート)、n−トリアコンタノエート(C30)、n−テトラコンタノエート(n−tetracontanoate)(C40)、シス−Δ9−オクタデカノエート(C18、オレエート)、全てのシス−Δ5,8,11,14−エイコサテトラエノエート(C20、アラキドネート)、オクタン二酸、テトラデカン二酸、オクタデカン二酸、ドコサン二酸などが包含される。適当な脂肪酸エステルには、線状もしくは分枝状の低級アルキル基を含んでなるジカルボン酸のモノエステルが包含される。低級アルキル基は、1〜約12個、好ましくは1〜約6個の炭素原子を含んでなることができる。
ティボディもしくはリガンド結合フラグメントはまた、ヒンジコアミメティボディもしくはリガンド結合フラグメントのジスルフィド結合(例えば、鎖内ジスルフィド結合)を還元することにより製造することもできる。次に、還元されたヒンジコアミメティボディもしくはリガンド結合フラグメントをチオール反応性改変剤と反応させて本発明の改変されたヒンジコアミメティボディを生成せしめることができる。本発明のヒンジコアミメティボディまたは特定の部分もしくはバリアントの特定の部位に結合している有機部分を含んでなる改変されたヒトミメティボディおよびリガンド結合フラグメントは、逆タンパク質分解(Fisch et al.,Bioconjugate Chem.,3:147−153(1992);Werlen et al.,Bioconjugate Chem.,5:411−417(1994);Kumaran et al.,Protein Sci.6(10):2233−2241(1997);Itoh et al.,Bioorg.Chem.,24(1):59−68(1996);Capellas et al.,Biotechnol.Bioeng.,56(4):456−463(1997))、およびHermanson,G.T.,Bioconjugate Techniques,Academic Press:San Diego,CA(1996)に記述されている方法のような、適当な方法を用いて製造することができる。
本発明はまた、天然に存在しない組成物、混合物もしくは形態で提供される本明細書に記述されるようなそして/もしくは当該技術分野において既知であるような、少なくとも1つ、少なくとも2つ、少なくとも3つ、少なくとも4つ、少なくとも5つ、少なくとも6つもしくはそれ以上のミメティボディまたはその特定の部分もしくはバリアントを含んでなる少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物も提供する。そのような組成物パーセンテージは、当該技術分野において既知であるようなもしくは本明細書に記述されるような、液体もしくは乾式の溶液、混合物、懸濁液、エマルジョンもしくはコロイドとしての重量、容量、濃度、モル濃度または重量モル濃度による。
平衡薬、血液製剤、抗腫瘍薬、免疫調節薬、点眼薬、点耳薬もしくは点鼻薬、局所用薬剤、栄養薬剤などの少なくとも1つから選択される少なくとも1つの化合物もしくはタンパク質の有効量をさらに含んでなることができる。本明細書に提示する各々の製剤、適応症、投薬および投与を包含する、そのような薬剤は、当該技術分野において周知である(例えば、各々引用することにより本明細書に全部が組み込まれる、Nursing 2001 Handbook of Drugs,21st edition,Springhouse Corp.,Springhouse,PA,2001;Health Professional’s Drug Guide 2001,ed.,Shannon,Wilson,Stang.Prentice−Hall,Inc,Upper Saddle River,NJ;Pharmcotherapy Handbook,Wells et al.,ed.,Appleton & Lange,Stamford,CTを参照)。
メチコン、重炭酸ナトリウムから選択される少なくとも1つであることができる。少なくとも1つの消化酵素もしくは胆石溶解剤は、パンクレアチン、パンクレリパーゼ、ウルソジオールから選択される少なくとも1つであることができる。少なくとも1つの下痢止め薬は、アタパルジャイト、次サリチル酸ビスマス、カルシウムポリカルボフィル、塩酸ジフェノキシレートもしくは硫酸アトロピン、ロペラミド、酢酸オクトレオチド、アヘンチンキ、アヘンチンキ(樟脳の入った)から選択される少なくとも1つであることができる。少なくとも1つの下剤は、ビソコジル(bisocodyl)、カルシウムポリカルボフィル、カスカラサグラダ、カスカラサグラダ芳香族流エキス剤、カスカラサグラダ流エキス剤、ヒマシ油、ドキュセートカルシウム、ドキュセートナトリウム、グリセリン、ラクツロース、クエン酸マグネシウム、水酸化マグネシウム、硫酸マグネシウム、メチルセルロース、鉱油、ポリエチレングリコールもしくは電解質溶液、オオバコ、センナ、リン酸ナトリウムから選択される少なくとも1つであることができる。少なくとも1つの制吐剤は、塩酸クロルプロマジン、ジメンヒドリネート、メシル酸ドラセトロン、ドロナビノール、塩酸グラニセトロン、塩酸メクリジン、塩酸メトクロプラミド(metocloproamide)、塩酸オンダンセトロン、ペルフェナジン、プロクロルペラジン、エジシル酸プロクロルペラジン、マレイン酸プロクロルペラジン、塩酸プロメタジン、スコポラミン、マレイン酸トリエチルペラジン、塩酸トリメトベンズアミドから選択される少なくとも1つであることができる。少なくとも1つの抗潰瘍薬は、シメチジン、塩酸シメチジン、ファモチジン、ランソプラゾール、ミソプロストール、ニザチジン、オメプラゾール、ラベプラゾール(rabeprozole)ナトリウム、ラニチジンクエン酸ビスマス、塩酸ラニチジン、スクラルフェートから選択される少なくとも1つであることができる。(例えば、Nursing 2001 Drug Handbookのpp.643〜95を参照。)
メクロレタミン、メルファラン、塩酸メルファラン、ストレプトゾシン、テモゾロマイド、チオテパから選択される少なくとも1つであることができる。少なくとも1つの代謝拮抗剤は、カペシタビン、クラドリビン、シタラビン、フロクスウリジン、リン酸フルダラビン、フルオロウラシル、ヒドロキシウレア、メルカプトプリン、メトトレキセート、メトトレキセートナトリウム、チオグアニンから選択される少なくとも1つであることができる。少なくとも1つの抗生物質抗腫瘍薬は、硫酸ブレオマイシン、ダクチノマイシン、クエン酸ダウノルビシンリポソーム製剤、塩酸ダウノルビシン、塩酸ドキソルビシン、塩酸ドキソルビシンリポソーム製剤、塩酸エピルビシン、塩酸イダルビシン、マイトマイシン、ペントスタチン、プリカマイシン、バルルビシンから選択される少なくとも1つであることができる。ホルモン平衡を改変する少なくとも1つの抗腫瘍薬は、アナストロゾール、ビカルタミド、エストラムスチンリン酸ナトリウム、エキセメスタン、フルタミド、酢酸ゴセレリン、レトロゾール、酢酸ロイプロリド、酢酸メゲストロール、ニルタミド、クエン酸タモキシフェン、テストラクトン、クエン酸トレミフェンから選択される少なくとも1つであることができる。少なくとも1つのその他の抗腫瘍薬は、アスパラギナーゼ、バシラス・カルメット−ゲラン(BCG)(生、膀胱内)、ダカルバジン、ドセタキセル、エトポシド、リン酸エトポシド、塩酸ジェムシタビン、塩酸イリノテカン、ミトタン、塩酸ミトキサントロン、パクリタキセル、ペグアスパルガーゼ、ポルフィマーナトリウム、塩酸プロカルバジン、リツキシマブ、テニポシド、塩酸トポテカン、トラスツズマブ、トレチノイン、硫酸ビンブラスチン、硫酸ビンクリスチン、酒石酸ビノレルビンから選択される少なくとも1つであることができる。(例えば、Nursing 2001 Drug Handbookのpp.867〜963を参照。)
少なくとも1つのビタミンもしくはミネラルは、ビタミンA、ビタミンB複合体、シアノコバラミン、葉酸、ヒドロキソコバラミン、ロイコボリンカルシウム、ナイアシン、ナイアシンアミド、塩酸ピリドキシン、リボフラビン、塩酸チアミン、ビタミンC、ビタミンD、コレカルシフェロール、エルゴカルシフェロール、ビタミンDアナログ、ドキセルカルシフェロール、パリカルシトール、ビタミンE、ビタミンKアナログ、フィトナジオン、フッ化ナトリウム、フッ化ナトリウム(局所)、微量元素、クロム、銅、ヨウ素、マンガン、セレン、亜鉛から選択される少なくとも1つであることができる。少なくとも1つのカロリー薬は、アミノ酸輸液(結晶)、デキストロースにおけるアミノ酸輸液、電解質を有するアミノ酸輸液、デキストロースにおける電解質を有するアミノ酸輸液、肝不全用アミノ酸輸液、高度代謝性侵襲用アミノ酸輸液、腎不全用アミノ酸輸液、デキストロース、脂肪乳剤、中鎖トリグリセリドから選択される少なくとも1つであることができる。(例えば、Nursing 2001 Drug Handbookのpp.1137〜63を参照。)
上記のように、本発明は、製薬学的に許容しうる製剤において少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントを含んでなる、好ましくは食塩水もしくは選択した塩を有する適当なバッファーを含むことができる安定な製剤、ならびに防腐剤を含有する任意の保存溶液および製剤ならびに製薬学的もしくは獣医学的用途に適当な多目的保存製剤を提供する。保存製剤は、水性希釈剤中に少なくとも1つの既知のもしくは場合により少なくとも1つのフェノール、m−クレゾール、p−クレゾール、o−クレゾール、クロロクレゾール、ベンジルアルコール、亜硝酸フェニル水銀、フェノキシエタノール、ホルムアルデヒド、クロロブタノール、塩化マグネシウム(例えば、6水和物)、アルキルパラベン(メチル、エチル、プロピル、ブチルなど)、塩化ベンザルコニウム、塩化ベンゼトニウム、デヒドロ酢酸ナトリウムおよびチメロサール、もしくはその混合物よりなる群から選択される防腐剤を含有する。0.001〜5%、またはその中の任意の範囲もしくは値、例えば、0.001、0.003、0.005、0.009、0.01、0.02、0.03、0.05、0.09、0.1、0.2、0.3、0.4、0.5、0.6、0.7、0.8,0.9、1.0、1.1、1.2、1.3、1.4、1.5、1.6,1.7、1.8、1.9、2.0、2.1、2.2、2.3、2.4、2.5、2.6、2.7、2.8、2.9、3.0、3.1、3.2、3.3、3.4、3.5、3.6、3.7、3.8、3.9、4.0、4.3、4.5、4.6、4.7、4.8、4.9、またはその中の任意の範囲もしくは値のような、しかしこれらに限定されるものではない、任意の適当な濃度もしくは混合物を当該技術分野において既知であるように用いることができる。限定されない例には、保存剤なし、0.1〜2%のm−クレゾール(例えば、0.2、0.3、0.4、0.5、0.9、1.0%)、0.1〜3%のベンジルアルコール(例えば、0.5、0.9、1.1、1.5、1.9、2.0、2.5%)、0.001〜0.5%のチメロサール(例えば、0.005、0.01)、0.001〜2.0%のフェノール(例えば、0.05、0.25、0.28、0.5、0.9、1.0%)、0.0005〜1.0%のアルキルパラベン(1つもしくは複数)(例えば、0.00075、0.0009、0.001、0.002、0.005、0.0075、0.009、0.01、0.02、0.05、0.075、0.09、0.1、0.2、0.3、0.5、0.75、0.9、1.0%)などが包含される。
液を調製するために、例えば、水もしくはバッファーにおける少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントの測定量を所望の濃度でタンパク質および場合により防腐剤もしくはバッファーを与えるために十分な量で合わせる。この方法のバリエーションは、当業者により認識される。例えば、成分を加える順序、追加の添加剤を使用するかどうか、製剤を調製する温度およびpHは全て、使用する濃度および投与の手段に関して最適化することができる因子である。
ミメティボディについての本発明はまた、任意の貧血、癌処置関連貧血、放射線療法もしくは化学療法関連貧血、ウイルスもしくは細菌感染処置関連貧血、腎性貧血、未熟児貧血、小児癌および/もしくは成人癌関連貧血、リンパ腫、骨髄腫、多発性骨髄腫と関連する貧血、エイズ関連貧血、待機手術を待っている自己献血があるもしくはない患者の同時処置、手術の術前および術後、自己献血もしくは輸血、術中管理、周期性好中球減少症もしくはコストマン症候群(先天的顆粒球減少症)、末期腎臓病、透析と関連する貧血、慢性腎不全、原発性造血疾患、例えば先天性形成不良性貧血、サラセミアメジャー、もしくは鎌状赤血球病、鎌状赤血球病の血管閉塞性合併症の少なくとも1つが包含されるがこれらに限定されるものではない細胞、組織、臓器、動物もしくは患者における貧血を調節するかもしくは処置する方法も提供する。Furman et al.,Pediatrics 1992;90:716−728,Goldberg Science.1988;242:1412−1415;Paul et al.,Exp Hematol.1984;12:825−830;Erslev et al.,Arch Intern
Med.1968;122:230−235;Ersley et al.,Ann Clin Lab Sci.1980;10:250−257;Jacobs et al.,Nature.1985;313:806−810;Lin et al.,Proc Natl Acad Sci USA.1985;82:7580−7584;Law et al.,Proc Natl Acad Sci USA.1986;83:6920−6924;Goldwasser et al.,J Biol Chem.1974;249:4202−4206;Eaves et al.,Blood.1978;52:1196−1210;Sawyer et al.,Blood.1989;74:103−109;Winearls et al.,Lancet.1986;2:1175−1178;Eschbach et al.,N Engl J Med.1987;316:73−78;Eschbach et al.,Ann Intern Med.1989;111:992−1000、各参考文献は引用することにより本明細書に全部が組み込まれる。
et al.,Immunol.Today,4:72−79(1983);Ausubel et al.,eds.Current Protocols in Molecular Biology,Wiley Interscience,New York(1987−2003);およびMuller,Meth.Enzymol.,92:589−601(1983)に見出されることができ、これらの参考文献は、引用することにより本明細書に全部が組み込まれる。
本発明において有用な好ましいTNF受容体分子は、高い親和性でTNFαに結合し(例えば、Feldmann et al.,国際公開第WO92/07076号(1992年4月30日公開);Schall et al.,Cell 61:361−370(1990);およびLoetscher et al.,Cell 61:351−359(1990)を参照、これらの参考文献は、引用することにより本明細書に全部が組み込まれる)、そして場合により低い免疫原性を有するものである。特に、55kDa(p55 TNF−R)および75kDa(p75 TNF−R)TNF細胞表面受容体は、本発明において有用である。受容体の細胞外ドメイン(ECD)もしくはその機能性部分(例えば、Corcoran et al.,Eur.J.Biochem.223:831−840(1994)を参照)を含んでなる、これらの受容体の切断型もまた、本発明において有用である。ECDを含んでなる、TNF受容体の切断型は、30kDaおよび40kDa TNFα阻害結合タンパク質として尿および血清において検出されている(Engelmann,H.et al.,J.Biol.Chem.265:1531−1536(1990))。TNF受容体マルチマー分子およびTNF免疫受容体融合分子、ならびにその誘導体およびフラグメントもしくは部分は、本発明の方法および組成物において有用であるTNF受容体分子のさらなる例である。本発明において用いることができるTNF受容体分子は、症状の良好ないし極めて優れた緩和および低い毒性で長期間にわたって患者を処置するそれらの能力を特徴とする。低い免疫原性および/もしくは高い親和性、ならびに他の定義されていない特性は、得られる治療結果に寄与し得る。
ことが必要である可能性があり、ここで、該個別投与は、所望の1日用量もしくは効果が得られるまで繰り返される。
本発明の少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントの治療的に有効な量を投与するために多数の既知のそして開発される形態を本発明に従って用いることできる。肺投与が以下の記述において用いられるが、他の投与形態を適当な結果で本発明に従って用いることができる。
非経口投与用の製剤は、一般的な賦形剤として滅菌水もしくは食塩水、ポリエチレングリコールのようなポリアルキレングリコール、植物由来の油、水素化ナフタレンなどを含有することができる。注入用の水性もしくは油性懸濁剤は、既知の方法に従って、適切な乳化剤もしくは加湿剤(humidifier)および沈殿防止剤を用いることにより製造することができる。注入剤は、水溶液または溶媒における滅菌した注入可能な溶液もしくは懸濁液のような無毒の非経口的に投与可能な希釈剤であることができる。使用可能な賦形剤もしくは溶媒として、水、リンガー溶液、等張食塩水などが認められ;通常の溶媒もしくは懸濁溶媒として、滅菌した不揮発性油を用いることができる。これらの目的のために、天然もしくは合成もしくは半合成の脂肪油もしくは脂肪酸;天然もしくは合成もしくは半合成のモノ−もしくはジ−もしくはトリグリセリドを包含する、任意の種類の不揮発性油および脂肪酸を用いることができる。非経口投与は当該技術分野において既知であり、そして通常の注入手段、米国特許第5,851,198号に記述されているようなガス加圧無針(gas pressured needle−less)注入装置、および引用することにより全部が本明細書に組み込まれる米国特許第5,839,446号に記述されているようなレーザー穿孔器装置が包含されるが、これらに限定されるものではない。
本発明はさらに、非経口、皮下、筋肉内、静脈内、ボーラス、膣、直腸、口腔、舌下、鼻腔内もしくは経皮手段による少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントの投与に関する。タンパク質、ヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物は、特に液体溶液もしくは懸濁液の形態で非経口(皮下、筋肉内もしくは静脈内)投与の使用のために;クリームおよび座薬のような特に半固体形態で膣もしくは直腸投与における使用のために;特に錠剤もしくはカプセル剤の形態で口腔もしくは舌下投与のために;あるいは特に粉末、点鼻薬もしくはエアロゾルまたはある種の作用因子の形態で鼻腔内に;あるいは皮膚構造を改変するためにもしくは経皮パッチにおける薬剤濃度を増加するためにジメチルスルホキシドのような化学エンハンサーを有する(引用することにより全部が本明細書に組み込まれる、Junginger,et al.“Drug Permeation Enhancement”;Hsieh,D.S.,Eds.,pp.59−90(Marcel Dekker,Inc.New York 1994)、あるいは皮膚上へのタンパク質およびペプチドを含有する製剤の使用(WO 98/53847)、または電気穿孔のような一時的輸送経路を作り出すためのもしくはイオン導入のような皮膚を通した荷電した薬剤の移動性を増加するための電場の使用、または超音波導入のような超音波の使用(米国特許第4,309,989号および第4,767,402号)を可能にする酸化剤を有する特にゲル、軟膏、ローション、懸濁液もしくはパッチ送達系の形態で経皮的に製造することができる(上記の公開および特許は、引用することにより全部が本明細書に組み込まれる)。
肺投与では、好ましくは少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物は、肺もしくは洞の下気道に到達するために有効な粒子サイズで送達される。本発明によれば、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントは、吸入による治療薬の投与に当該技術分野において既知である様々な吸入もしくは点鼻装置のいずれかにより送達することができる。患者の洞腔(sinus cavity)もしくは肺胞にエアロゾル化した製剤を置くことができるこれらの装置には、定量吸入器、ネブライザー、ドライパウダー発生器、スプレーなどが包含される。ヒンジコアミメティボディまたは特定の部分もしくはバリアントの肺もしくは鼻腔投与を導くために適当な他の装置もまた、当該技術分野において既知である。全てのそのような装置は、エアロゾルにおけるヒンジコアミメティボディまたは特定の部分もしくはバリアントの施薬のための投与に適当な製剤のものを用いることができる。そのようなエアロゾルは、溶液(水性および非水性の両方)もしくは固体粒子のいずれかを含んでなることができる。VentolinR定量吸入器のような定量吸入器は、典型的に噴射ガスを使用し、そして吸気中の作動を必要とする(例えば、WO 94/16970、WO
98/35888を参照)。TurbuhalerTM(Astra)、RotahalerR(Glaxo)、DiskusR(Glaxo)、SpirosTM吸入器(Dura)、Inhale Therapeuticsにより市販される装置、およびSpinhalerRパウダー吸入器(Fisons)のようなドライパウダー吸入器は、混合パウダーの呼吸作動を用いる(引用することにより本明細書に全部が組み込まれる、US 4668218 Astra,EP 237507 Astra,WO 97/25086 Glaxo,WO 94/08552 Dura,US 5458135 Inhale,WO 94/06498 Fisons)。AERxTM Aradigm、UltraventRネブライザー(Mallinckrodt)、およびAcorn IIRネブライザー(Marquest Medical Products)(US 5404871 Aradigm,WO 97/22376)(上記の参考文献は、引用することにより全部が本明細書に組み込まれる)のようなネブライザーは、溶液からエアロゾルを生成し、一方、定量吸入器、ドライパウダー吸入器などは、小粒子エアロゾルを生成する。市販されている吸入装置のこれらの特定の例は、本発明の実施に適当な特定の装置の代表であるものとし、そして本発明の範囲を限定するものではない。好ましくは、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントを含んでなる組成物は、ドライパウダー吸入器もしくはスプレーにより送達される。本発明の少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントを投与するための吸入装置のいくつかの望ましい特徴がある。例えば、吸入装置による送達は、都合よく信頼性があり、再現可能であり、そして正確である。吸入装置は、場合により、十分に呼吸が可能であるように、例えば約10μm未満、好ましくは約1〜5μmの小乾燥粒子を送達することができる。
ヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質を含むスプレーは、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントの懸濁液もしくは溶液を圧力下でノズルを通して押し出すことにより製造することができる。ノズルのサイズおよび構造、適用圧力、ならびに液体供給速度は、所望の出力および粒子サイズを得るために選択することができる。例えば、毛細管もしくはノズル送りと接続した電場によりエレクトロスプレーを生成することができる。都合よく、スプレーにより送達される少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質の粒子は、約10μm未満、好ましくは約1μm〜約5μmの範囲、そして最も好ましくは約2μm〜約3μmの粒子サイズを有する。
ヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質は、ジェットネブライザーもしくは超音波ネブライザーのような、ネブライザーにより投与することができる。典型的に、ジェットネブライザーでは、開口部を通して高速空気ジェットを作り出すために圧縮空気源が用いられる。気体がノズルを越えて広がるにつれて、低圧領域が生み出され、それは液体リザーバーに接続されている毛細管を通してヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質の溶液を引き出す。毛細管からの液体の流れは、それが管から抜け出るにつれて不安定なフィラメントおよび小滴に剪断され、エアロゾルを生み出す。既定のジェットネブライザーから所望の性能特性を得るために一連の構造、流速およびバッフルタイプを用いることができる。超音波ネブライザーでは、典型的に圧電変換器を使用して、振動の、機械的エネルギーを生み出すために高周波電気エネルギーを用いる。このエネルギーは、直接もしくはカップリング流動体を通してヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質の製剤に伝達され、ヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質を含むエアロゾルを生み出す。都合よく、ネブライザーにより送達されるヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質の粒子は、約10μm未満、好ましくは約1μm〜約5μmの範囲、そして最も好ましくは約2μm〜約3μmの粒子サイズを有する。
定量吸入器(MDI)において、噴射剤、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアント、および任意の賦形剤もしくは他の添加剤を、液化圧縮ガスを含む混合物として容器に含有する。計量弁の作動により、好ましくは、約10μm未満、好ましくは約1μm〜約5μm、そして最も好ましくは約2μm〜約3μmのサイズ範囲の粒子を含有する、エアロゾルとして混合物が放出される。所望のエアロゾル粒子サイズは、ジェットミル(jet−milling)、噴霧乾燥、臨界点凝縮などを包含する、当業者に既知である様々な方法により製造されるヒンジコアミメティボディまたは特定の部分もしくはバリアント組成物タンパク質の製剤を用いることにより得られることができる。好ましい定量吸入器には、3MもしくはGlaxoにより製造されそしてヒドロフルオロカーボン噴射剤を用いるものが包含される。
ィまたは特定の部分もしくはバリアントを含有する微粉化粉末が包含される。噴射剤は、トリクロロフルオロメタン、ジクロロジフルオロメタン、ジクロロテトラフルオロエタノールおよび1,1,1,2−テトラフルオロエタン、HFA−134a(ヒドロフルオロアルカン−134a)、HFA−227(ヒドロフルオロアルカン−227)などを包含する、クロロフルオロカーボン、ヒドロクロロフルオロカーボン、ヒドロフルオロカーボンもしくは炭水化物のような、この目的のために用いられる任意の通常の物質であることができる。好ましくは、噴射剤はヒドロフルオロカーボンである。界面活性剤は、噴射剤における懸濁液として少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントを安定させるため、化学分解から有効成分を守るためなどに選択することができる。適当な界面活性剤には、ソルビタントリオレエート、ダイズレシチン、オレイン酸などが包含される。ある場合には、エタノールのような溶媒を用いる溶液エアロゾルが好ましい。タンパク質のようなタンパク質の調合用に当該技術分野において既知である追加の作用因子もまた、製剤に含むことができる。
粘膜面を通した吸収には、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントを投与する組成物および方法は、エマルジョン粒子の粘膜接着を成し遂げることにより粘膜面を通した吸収を促進する、複数のサブミクロン粒子、粘膜接着性高分子、生物活性ペプチドおよび水性連続相を含んでなるエマルジョンを含む(米国特許第5,514,670号)。本発明のエマルジョンの使用に適当な粘膜面には、角膜、結膜、口腔、舌下、鼻腔内、膣、肺、胃、腸および直腸投与経路を包含することができる。膣もしくは直腸投与用の製剤、例えば座薬は、賦形剤として例えばポリアルキレングリコール、ワセリン、ココアバターなどを含有することができる。鼻腔内投与用の製剤は固体であることができ、そして賦形剤として例えばラクトースを含有することができ、または点鼻薬の水性もしくは油性溶液であることができる。口腔投与では、賦形剤には糖、ステアリン酸カルシウム、ステアリン酸マグネシウム、アルファ化(pregelinatined)澱粉などが包含される(米国特許第5,849,695号)。
経口用製剤は、腸壁の透過性を人工的に増加するために添加剤(例えば、レゾルシノールならびにポリオキシエチレンオレイルエーテルおよびn−ヘキサデシルポリエチレンエーテルのような非イオン性界面活性剤)の共投与、ならびに酵素分解を阻止するために酵素インヒビター(例えば、膵臓トリプシンインヒビター、ジイソプロピルフルオロリン酸塩(DFF)およびトラジロール)の共投与に依存する。経口投与用の固形タイプ投与形態物の有効成分化合物は、ショ糖、ラクトース、セルロース、マンニトール、トレハロース、ラフィノース、マルチトール、デキストラン、澱粉、寒天、アルギン酸塩、キチン、キトサン、ペクチン、トラガカントゴム、アラビアゴム、ゼラチン、コラーゲン、カゼイン、アルブミン、合成もしくは半合成ポリマー、およびグリセリドを包含する、少なくとも1つの添加剤と混合することができる。これらの投与形態物はまた、他のタイプ(1つもしくは複数)の添加剤、例えば、不活性希釈剤、ステアリン酸マグネシウム、パラベンのような潤滑剤、ソルビン酸、アスコルビン酸、アルファ−トコフェロールのような防腐剤、システインのような酸化防止剤、崩壊剤、結合剤、増粘剤、緩衝剤、甘味料、着香料、香料などを含有することもできる。
および液剤製剤が包含される。これらの製剤は、該分野において通常用いられる不活性希釈剤、例えば水を含有することができる。リポソームもまた、インシュリンおよびヘパリンの薬剤送達系として記述されている(米国特許第4,239,754号)。さらに最近では、混合アミノ酸の人工ポリマーの微小球(プロテイノイド)が医薬品を送達するために用いられている(米国特許第4,925,673号)。さらに、米国特許第5,879,681号および米国特許第5,871,753号に記述されているキャリア化合物は、生物活性因子を経口的に送達するために用いられ、当該技術分野において既知である。
経皮投与には、少なくとも1つのヒンジコアミメティボディまたは特定の部分もしくはバリアントは、リポソームもしくはポリマーナノ粒子、微粒子、マイクロカプセル、または微小球(他に記載されない限りまとめて微粒子と称する)のような送達装置に封入される。ポリ乳酸、ポリグリコール酸およびそのコポリマーのようなポリヒドロキシ酸、ポリオルトエステル、ポリ無水物、およびポリホスファゼンのような合成ポリマー、ならびにコラーゲン、ポリアミノ酸、アルブミンおよび他のタンパク質、アルギン酸塩および他の多糖のような天然ポリマー、ならびにその組み合わせでできている微粒子を包含する、多数の適当な装置が既知である(米国特許第5,814,599号)。
本発明の化合物を被験体に長期間にわたって、例えば単回投与から1週〜1年の期間にわたって送達することが望ましいことがあり得る。様々な持続放出、デポーもしくは埋め込み投与形態物を利用することができる。例えば、投与形態物は、体液において低い程度の溶解性を有する化合物の製薬学的に許容しうる無毒の塩、例えば、(a)リン酸、硫酸、クエン酸、酒石酸、タンニン酸、パモン酸、アルギン酸、ポリグルタミン酸、ナフタレンモノもしくはジスルホン酸、ポリガラクツロン酸などのような多塩基酸との酸付加塩;(b)亜鉛、カルシウム、ビスマス、バリウム、マグネシウム、アルミニウム、銅、コバルト、ニッケル、カドミウムなどのような多価金属陽イオンとの、または例えばN,N’−ジベンジル−エチレンジアミンもしくはエチレンジアミンから形成される有機陽イオンとの塩;あるいは(c)(a)および(b)の組み合わせ、例えばタンニン酸亜鉛塩を含有することができる。さらに、本発明の化合物もしくは好ましくは今記述したもののような比較的不溶性の塩は、ゲル、例えば、注入に適当な、例えばゴマ油を有するモノステアリン酸アルミニウムゲルにおいて調合することができる。特に好ましい塩は、亜鉛塩、タンニン酸亜鉛塩、パモン酸塩などである。注入用の持続放出デポー製剤の別のタイプは、例えば米国特許第3,773,919号に記述されているようなポリ乳酸/ポリグリコール酸ポリマーのようなゆっくり分解する無毒の非抗原性ポリマーにおける封入のために分散された化合物もしくは塩を含有する。化合物もしくは好ましくは上記のもののような比較的不溶性の塩はまた、特に動物における使用のために、コレステロールマトリックスシラスティックペレットにおいて調合することもできる。さらなる持続放出、デポーもしくは埋め込み製剤、例えば、気体もしくは液体リポソームは、文献において既知である(米国特許第5,770,222号および“Sustained and Controlled Release Drug Delivery Systems”,J.R.Robinson ed.,Marcel Dekker,Inc.,N.Y.,1978)。
[実施例]
典型的な哺乳類発現ベクターは、mRNAの転写の開始を媒介する少なくとも1つのプロモーター要素、ヒンジコアミメティボディまたは特定の部分もしくはバリアントコーディング配列、ならびに転写の終結および転写産物のポリアデニル化に必要なシグナルを含有する。追加の要素には、エンハンサー、コザック配列ならびにRNAスプライシングの供与および受容部位が隣接する介在配列が包含される。非常に効率のよい転写は、SV40からの初期および後期プロモーター、レトロウイルス、例えば、RSV、HTLVI、HIVIからの長い末端反復(LTR)ならびにサイトメガロウイルス(CMV)の初期プロモーターで成し遂げることができる。しかしながら、細胞要素もまた用いることができる(例えば、ヒトアクチンプロモーター)。本発明を実施することにおいて使用する適当な発現ベクターには、例えば、pIRES1neo、pRetro−Off、pRetro−On、PLXSNもしくはpLNCX(Clontech Labs,Palo Alto,CA)、pcDNA3.1(+/−)、pcDNA/Zeo(+/−)もしくはpcDNA3.1/Hygro(+/−)(Invitrogen)、PSVLおよびPMSG(Pharmacia,Uppsala,Sweden)、pRSVcat(ATCC 37152)、pSV2dhfr(ATCC 37146)およびpBC12MI(ATCC 67109)のようなベクターが包含される。用いることができる哺乳類宿主細胞には、ヒトHela 293、H9およびJurkat細胞、マウスNIH3T3およびC127細胞、Cos1、Cos7およびCV1、ウズラQC1−3細胞、マウスL細胞ならびにチャイニーズハムスター卵巣(CHO)細胞が包含される。
ヒンジコアミメティボディまたは特定の部分もしくはバリアントの発現にベクターpC4を用いる。プラスミドpC4は、プラスミドpSV2−dhfr(ATCC受託番号37146)の誘導体である。該プラスミドは、SV40初期プロモーターの制御下でマウスDHFR遺伝子を含有する。これらのプラスミドでトランスフェクションするジヒドロ葉酸活性を欠いているチャイニーズハムスター卵巣細胞もしくは他の細胞は、化学療法剤メトトレキセートを補足した選択培地(例えば、アルファマイナスMEM、Life Technologies,Gaithersburg,MD)において細胞を培養することにより選択することができる。メトトレキセート(MTX)に耐性の細胞におけるDHFR遺伝子の増幅は、十分に立証されている(例えば、F.W.Alt,et al.,J.Biol.Chem.253:1357−1370(1978);J.L.Hamlin and C.Ma,Biochem.et Biophys.Acta 1097:107−143(1990);およびM.J.Page and M.A.Sydenham,Biotechnology 9:64−68(1991)を参照)。増加する濃度のMTXにおいて培養した細胞は、DHFR遺伝子の増幅の結果として、標的酵素DHFRを過剰生産することにより薬剤に対する耐性を生じる。第二の遺伝子をDHFR遺伝子に連結する場合、それは通常共増幅され、そして過剰発現される。この方法は、1,000コピーより多くの増幅遺伝子(1つもしくは複数)を保有する細胞系を開発するために使用できることが当該技術分野において既知である。次に、メトトレキセートを中止すると、宿主細胞の1つもしくはそれ以上の染色体に組み込まれた増幅遺伝子を含有する細胞系が得られる。
1 Blue細胞を形質転換し、そして例えば制限酵素分析を用いて、プラスミドpC4に挿入されたフラグメントを含有する細菌を同定する。
つの重要な決定要因は、MHC分子により効率よく結合されそしてT細胞に提示されるそして細胞に基づく免疫応答もしくは抗体応答のためのT細胞介助を引き出すタンパク質由来のペプチドの能力である。MHC結合の公的に利用可能なウェブ上のアルゴリズム(SYFPETHI,Ramensee et al.,1999,Immunogenetics,vol.50,213−19およびBIMAS)を用いて、ミメティボディ内の潜在的MHC結合エピトープを分析した。1つもしくはそれ以上のペプチドの予測される免疫原性を減少する突然変異は、免疫原性へのインビボ効果について評価される。
利点:上記のミメティボディ構築物は、生物活性ペプチドを提示する別の方法を提供する。さらに、提示される改変は、本発明のミメティボディの新規な特徴と組み合わせてそしてそれに加えて、それらの有用性を高めると予想される。
Claims (24)
- 式(I):
((V(m)−P(n)−L(o)−H(p)−CH2(q)−CH3(r))(s)
[式中、Vは免疫グロブリン可変領域のN末端の少なくとも1つの部分であり、Pは少なくとも1つの生物活性ペプチドであり、Lはリンカー配列であり、Hは免疫グロブリン可変ヒンジ領域の少なくとも1つの部分であり、CH2は免疫グロブリンCH2定常領域の少なくとも1つの部分であり、CH3は免疫グロブリンCH3定常領域の少なくとも1つの部分であり、そしてm、n、o、p、q、rおよびsは独立して0、1もしくは2〜10の間の任意の整数であることができる]
のポリペプチドをコードする少なくとも1つのポリヌクレオチドを含んでなる少なくとも1つのヒンジコアミメティボディ核酸。 - 式(I):
((V(m)−P(n)−L(o)−H(p)−CH2(q)−CH3(r))(s)
[式中、Vは免疫グロブリン可変領域のN末端の少なくとも1つの部分であり、Pは配列番号:43〜518から選択される少なくとも1つの生物活性ペプチドであり、Lはリンカー配列であり、Hは免疫グロブリン可変ヒンジ領域の少なくとも1つの部分であり、CH2は免疫グロブリンCH2定常領域の少なくとも1つの部分であり、CH3は免疫グロブリンCH3定常領域の少なくとも1つの部分であり、nおよびmは独立して0、1もしくは2〜10の間の整数であることができる]
のポリペプチドを含んでなる少なくとも1つのヒンジコアミメティボディポリペプチド。 - 式(I):
((V(m)−P(n)−L(o)−H(p)−CH2(q)−CH3(r))(s)
[式中、Vは免疫グロブリン可変領域のN末端の少なくとも1つの部分であり、Pは配列番号:519〜979から選択される少なくとも1つの生物活性ペプチドであり、Lはリンカー配列であり、Hは免疫グロブリン可変ヒンジ領域の少なくとも1つの部分であり、CH2は免疫グロブリンCH2定常領域の少なくとも1つの部分であり、CH3は免疫グロブリンCH3定常領域の少なくとも1つの部分であり、nおよびmは独立して0、1もしくは2〜10の間の整数であることができる]
のポリペプチドを含んでなる少なくとも1つのヒンジコアミメティボディポリペプチド。 - 該ポリペプチドが少なくとも1つのPポリペプチドの少なくとも1つの活性を有する請求項1に記載のヒンジコアミメティボディ核酸もしくはヒンジコアミメティボディポリペプチド。
- 請求項1に記載の少なくとも1つのヒンジコアミメティボディポリペプチドに特異的に結合する、モノクローナルもしくはポリクローナル抗体、融合タンパク質、またはそのフラグメントを含んでなるヒンジコアミメティボディ抗体。
- 請求項1に記載の少なくとも1つのヒンジコアミメティボディポリペプチドもしくはヒンジコアミメティボディ抗体をコードするヒンジコアミメティボディ核酸。
- 請求項6に記載の少なくとも1つの単離された核酸を含んでなるヒンジコアミメティボディベクター。
- 請求項7に記載の単離された核酸を含んでなるヒンジコアミメティボディ宿主細胞。
- 該宿主細胞がCOS−1、COS−7、HEK293、BHK21、CHO、BSC−
1、Hep G2、653、SP2/0、293、NSO、DG44 CHO、CHO K1、HeLa、骨髄腫もしくはリンパ腫細胞、またはその任意の誘導体、不死化もしくはトランスフォーム細胞から選択される少なくとも1つである、請求項8に記載のヒンジコアミメティボディ宿主細胞。 - ヒンジコアミメティボディもしくは抗体が検出可能なもしくは回収可能な量で発現されるように、インビトロ、インビボもしくはin situにおける条件下で請求項6に記載の核酸を翻訳することを含んでなる、少なくとも1つのヒンジコアミメティボディポリペプチドもしくはヒンジコアミメティボディ抗体を製造する方法。
- 請求項1に記載の少なくとも1つのヒンジコアミメティボディ核酸、ヒンジコアミメティボディポリペプチドもしくはヒンジコアミメティボディ抗体を含んでなる組成物。
- 該組成物が少なくとも1つの製薬学的に許容しうる担体もしくは希釈剤をさらに含んでなる請求項11に記載の組成物。
- 検出可能な標識もしくはレポーター、TNFアンタゴニスト、抗感染症薬、心臓血管(CV)系薬、中枢神経系(CNS)薬、自律神経系(ANS)薬、気道薬、胃腸(GI)管薬、ホルモン薬、体液もしくは電解質平衡薬、血液製剤、抗腫瘍薬、免疫調節薬、点眼薬、点耳薬もしくは点鼻薬、局所用薬剤、栄養薬剤、サイトカインまたはサイトカインアンタゴニストの少なくとも1つから選択される少なくとも1つの化合物、組成物もしくはポリペプチドの治療的に有効な量を含んでなる少なくとも1つの組成物をさらに含んでなる請求項11に記載の組成物。
- 液体、気体、もしくは乾式の、溶液、混合物、懸濁液、エマルジョンもしくはコロイド、凍結乾燥標品、または粉末から選択される少なくとも1つの形態の請求項11に記載の組成物。
- (a)請求項1に記載の少なくとも1つのヒンジコアミメティボディ核酸、ポリペプチドもしくは抗体の有効量を含んでなる組成物を当該細胞、組織、臓器もしくは動物と接触させるかもしくはそれに投与すること
を含んでなる細胞、組織、臓器もしくは動物におけるヒンジコアミメティボディリガンド関連症状を診断するかもしくは処置する方法。 - 該有効量が該細胞、組織、臓器もしくは動物のキログラム当たり0.001〜50mgのヒンジコアミメティボディ抗体;0.000001〜500mgの該ヒンジコアミメティボディ;もしくは0.0001〜100μgの該ヒンジコアミメティボディ核酸である請求項15に記載の方法。
- 該接触させることもしくは該投与することが、非経口、皮下、筋肉内、静脈内、関節内、気管支内、腹内、嚢内、軟骨内、腔内(intracavitary)、腔内(intracelial)、小脳(intracelebellar)内、脳室内、結腸内、頸内、胃内、肝臓内、心筋内、骨内、骨盤内、心膜内、腹腔内、胸膜腔内、前立腺内、肺内、直腸内、腎臓内、網膜内、脊椎内、滑液包内、胸内、子宮内、膀胱内、病巣内、ボーラス、膣、直腸、口腔、舌下、鼻腔内もしくは経皮から選択される少なくとも1つの形態によってである請求項15に記載の方法。
- 該(a)接触させることもしくは投与することの前に、同時にもしくは後に、検出可能な標識もしくはレポーター、TNFアンタゴニスト、抗感染症薬、心臓血管(CV)系薬、中枢神経系(CNS)薬、自律神経系(ANS)薬、気道薬、胃腸(GI)管薬、ホル
モン薬、体液もしくは電解質平衡薬、血液製剤、抗腫瘍薬、免疫調節薬、点眼薬、点耳薬もしくは点鼻薬、局所用薬剤、栄養薬剤、サイトカインまたはサイトカインアンタゴニストの少なくとも1つから選択される少なくとも1つの化合物もしくはポリペプチドの有効量を含んでなる少なくとも1つの組成物を投与することをさらに含んでなる請求項15に記載の方法。 - 非経口、皮下、筋肉内、静脈内、関節内、気管支内、腹内、嚢内、軟骨内、腔内(intracavitary)、腔内(intracelial)、小脳内、脳室内、結腸内、頸内、胃内、肝臓内、心筋内、骨内、骨盤内、心膜内、腹腔内、胸膜腔内、前立腺内、肺内、直腸内、腎臓内、網膜内、脊椎内、滑液包内、胸内、子宮内、膀胱内、病巣内、ボーラス、膣、直腸、口腔、舌下、鼻腔内もしくは経皮から選択される少なくとも1つの形態により、該少なくとも1つの該ヒンジコアミメティボディポリペプチド、抗体もしくは核酸を接触させることもしくは投与することに適当である、請求項1に記載の少なくとも1つの単離されたヒンジコアミメティボディポリペプチド、抗体もしくは核酸を含んでなる装置。
- 包装材料および請求項1に記載の少なくとも1つの単離されたヒンジコアミメティボディポリペプチド、抗体もしくは核酸を含んでなる容器を含んでなる、ヒト製薬学的もしくは診断用途のための製品。
- 該容器が非経口、皮下、筋肉内、静脈内、関節内、気管支内、腹内、嚢内、軟骨内、腔内(intracavitary)、腔内(intracelial)、小脳内、脳室内、結腸内、頸内、胃内、肝臓内、心筋内、骨内、骨盤内、心膜内、腹腔内、胸膜腔内、前立腺内、肺内、直腸内、腎臓内、網膜内、脊椎内、滑液包内、胸内、子宮内、膀胱内、病巣内、ボーラス、膣、直腸、口腔、舌下、鼻腔内もしくは経皮送達装置もしくは系の成分である請求項20の製品。
- 該ポリペプチド、抗体もしくは核酸を検出可能なもしくは回収可能な量で発現することができる少なくとも1つの宿主細胞、トランスジェニック動物、トランスジェニック植物、植物細胞を提供することを含んでなる、請求項1に記載の少なくとも1つの単離されたヒンジコアミメティボディポリペプチド、抗体もしくは核酸を製造する方法。
- 請求項22に記載の方法により製造される少なくとも1つのヒンジコアミメティボディポリペプチド、抗体もしくは核酸。
- 本明細書に提示される開示に基づく任意の発明。
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- 2008-08-26 US US12/229,882 patent/US7705149B2/en not_active Expired - Lifetime
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