JPH1121293A - 非常に大規模な固定化ペプチドの合成 - Google Patents
非常に大規模な固定化ペプチドの合成Info
- Publication number
- JPH1121293A JPH1121293A JP8324451A JP32445196A JPH1121293A JP H1121293 A JPH1121293 A JP H1121293A JP 8324451 A JP8324451 A JP 8324451A JP 32445196 A JP32445196 A JP 32445196A JP H1121293 A JPH1121293 A JP H1121293A
- Authority
- JP
- Japan
- Prior art keywords
- substrate
- light
- amino acid
- mask
- receptor
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
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- C08G—MACROMOLECULAR COMPOUNDS OBTAINED OTHERWISE THAN BY REACTIONS ONLY INVOLVING UNSATURATED CARBON-TO-CARBON BONDS
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Abstract
ーニングのための新規な装置及び方法の提供。 【解決手段】 表面を有する基体を含んで成るポリマー
をスクリーニングするための装置であって、該表面は少
なくとも2個のあらかじめ定められた領域を含んで成
り、該あらかじめ定められた領域はその上に異るモノマ
ー配列を含み、該あらかじめ定められた領域の各々が約
0.1cm2 未満の面積を占めることを特徴とする装置。
Description
及び配置に関する。特に、本発明の1つの態様は単一基
体表面上の既知の場所における種々の化学配列の製造の
ための方法及び関連する装置を提供する。本発明は例え
ばオリゴマー、ペプチド、核酸、オリゴサッカライド、
ホスホリピド、ポリマー又は薬剤同類調製物の製造の分
野において、特に生物活性についてのスクリーニングに
おいて使用するための化学的多様性の源を創製するため
に適用され得る。構造と分子の活性との関係は生物学的
系の研究における基本的な事項である。構造−活性関係
は酵素の機能、細胞が相互に連絡し合う方法、並びに細
胞制御及びフィードバック系を理解するために重要であ
る。
元空間的及び電子的分布を有する他の分子と相互作用し
そして結合することが知られている。この様な特異性を
有するすべての大分子は、それが代謝中間体の加水分解
を触媒する酵素であるか、イオンの膜輸送を仲介する細
胞表面蛋白質であるか、近隣の細胞に対して特定の細胞
を同定するのに役立つ糖蛋白質であるか、血漿中で循環
しているIgG−クラス抗体であるか、核内のDNAの
オリゴヌクレオチド配列であるか等に拘らず、受容体
(receptor)と考えることができる。受容体が
選択的に結合する種々の分子はリガンド(ligan
d)として知られる。
測定するために多くの測定方法が利用可能であるが、こ
の様な実験から得られる情報は利用可能なリガンドの数
及びタイプによりしばしば制限される。新規なリガンド
は時として、偶然に、又はX−線結晶像分析及び蛋白質
のための遺伝子組換技法を含めて、分子構造の解明のた
めの新たな技法の適用により発見される。
関連性を探求するための例示的系である。ペプチドはア
ミノ酸の配列である。20種類の天然アミノ酸がポリマ
ー分子に縮合されるとき、それらは広範囲の種類の三次
元構造を形成し、それぞれは特定のアミノ酸配列及び溶
剤条件に基く。20種類の天然アミノ酸の可能なペンタ
ペプチドの数は、例えば205 又は3,200,000
の異るペプチドである。このサイズの分子が受容体結合
研究において有用であるらしいことは、幾つかの抗体が
数個のアミノ酸という短い配列を高い特異性をもって認
識することを示すエピトープ分析研究により支持され
る。さらに、アミノ酸の平均分子量は小ペプチドを、多
くの現在有用な医薬製剤のサイズ範囲に置く。
研究に頼る研究の1つのタイプである。ほとんどの場
合、生物学的に重要な受容体に対する特異性の望ましい
パターンを有する新規なリガンドを発見する過程とし
て、同時代的医薬研究を記載することができる。他の例
は、農業において使用するための新規な化合物、例えば
殺虫剤及び除草剤を発見するための研究である。時とし
て、リガンドを設計するための合理的な工程の解決は困
難であり又は弾力性に欠けるものである。多数の異るポ
リマーを調製するための従来の方法は、効果的で合理的
な又はランダムなスクリーニングを可能にするのに十分
な規模で用いられる場合、骨が折れるほど遅かった。例
えば、固体支持体上でのペプチドの合成のためにメリフ
ィールド(Merrifield)法(J.Am.Chem.Soc.
(1963) 85:2149-2154)が使用されている。
溶性ポリマーから作られた支持体に共有結合される。α
−保護基を有する他のアミノ酸が、前記共有結合したア
ミノ酸と反応してジペプチドを形成する。洗浄の後、保
護基が除去され、そしてα−保護基を有する第三のアミ
ノ酸が前記ジペプチドに加えられる。この工程は、所望
の長さ及び配列のペプチドが得られるまで続けられる。
メリフィールド法を用いる場合、1日に百を越えるペプ
チド配列を合成することは経済的に実際的ではない。
ポリマー合成のための一連の反応容器を使用することも
提案されている。例えば、試薬の自動化された逐次的付
加により固相支持体上で直鎖状ポリマーを合成するため
にチューブ状反応系を用いることができる。この方法は
なお、効果的で経済的なスクリーニングのために十分な
だけ多数のポリマー配列の合成を可能にしない。多数の
配列を調製するための方法が更に知られており、この方
法においては孔状(foraminous)容器が既知
量の反応性粒子を封入しており、この粒子は該容器の孔
より大きなサイズを有する。この容器は所望の材料と選
択的に反応して生成分分子の所望の配列を合成すること
ができる。当業界において知られている他の方法の場合
と同様に、この方法は、効果的なスクリーニングのため
に十分に多様なポリペプチドを合成するために特に用い
ることができない。
には、標準的マイクロタイタープレートの方式に合致す
る96個のプラスチックピン上でのペプチドの合成が含
まれる。不都合なことには、これらの技法はある程度有
用ではあるが実質的な問題点が残ったままである。例え
ば、これらの方法は、経済的に合成することができスク
リーニングすることができる配列の多様性において制限
されたままである。以上のことから、知られた場所にお
いて種々の化学的配列を合成するための改良された方法
及び装置が求められている。
た方法及び装置が開示される。1つの好ましい態様にお
いては、リンカー分子が基体上に与えられる。このリン
カー分子の一端には、光除去可能な(photorem
ovable)保護基により保護された反応性官能基が
設けられる。リソグラフ(lithography)法
を用いて、第一の選択された領域において、光除去可能
な保護基が光に暴露されそしてリンカー分子から除去さ
れる。次に基体を洗浄し、又は単一モノマーと接触せし
める。この第一モノマーはリンカー分子上の露出された
官能基と反応する。好ましい態様においては、モノマー
はそのアミノ末端又はカルボキシ末端に光除去可能な保
護基を含むアミノ酸であり、そしてリンカー分子は光除
去可能な保護基を担持するアミノ基又はカルボキシ酸基
を末端として有する。
暴露し、そしてリンカー分子/保護されたアミノ酸上の
光除去可能な保護基を該第二セットの領域において除去
する。次に、基体を、暴露された官能基との反応のため
に光除去可能な保護基を含有する第二モノマーと接触せ
しめる。所望の長さ及び所望の化学配列を有するポリマ
ーが得られるまで選択的にモノマーを適用するためにそ
の工程を反復する。次に、光感受性基を場合によっては
除去し、そして次に配列を場合によってはキャップす
る。側鎖保護基が存在する場合はそれらも除去される。
本明細書に開示するリソグラフ法を用いることにより、
基体上の相対的に小さな且つ正確に知られた場所に光を
向けることが可能である。従って、基体上の知られた場
所において知られた化学配列のポリマーを合成すること
が可能である。
いて多数のポリマーをスクリーニングすることを含めて
種々の用途を有するであろう。生物学的活性をスクリー
ニングするためには、基体を1又は複数の受容体、例え
ば抗体、全体細胞、小胞上の受容体、脂質、又は他の種
々の受容体のいずれかに暴露する。受容体は好ましくは
例えば蛍光標識、放射能標識、又は受容体と反応性の標
識された抗体により標識される。基体上の標識の位置は
例えば光子検出法又はオートラジオグラフィー法により
検出される。
の知識を通して、どの配列が受容体を結合するかを迅速
に決定することができ、そしてそれ故にこの技法を用い
て多数のペプチドをスクリーニングすることができる。
本発明の他の可能な用途には診断が含まれ、この場合、
特定の受容体に対する種々の抗体が基体上に置かれ、そ
して例えば血清が免疫不全についてスクリーニングされ
るであろう。更なる用途には、例えば、半導体装置にお
ける有機物質の選択的「ドーピング」(doping)
等が含まれる。
合成するための選択された反応器系も開示される。この
反応器系は、周辺付近で基体と適合する基体台を含む。
この基体台は基体と該台との間に反応器空間を備えてお
り、それを通して又はその中に反応流体がポンプ輸送さ
れ又は流れる。反応器空間中の基体の選択された領域を
脱保護するように、基体上にマスクが置かれ又は集中さ
れ、そして照明される。モノマーが反応器空間を通って
ポンプ輸送され又は基体と接触され、そして脱保護され
た領域と反応する。基体上の領域を選択的に脱保護し、
そして反応空間を通して所定のモノマーを流すことによ
り、知られた場所において所望のポリマーを合成するこ
とができる。
る。この検出方法及び装置は、基体の表面上の知られた
位置に非常に多様なポリマー配列を有する基体を用い
る。基体は蛍光標識された受容体に暴露され、該受容体
は1又は複数のポリマー配列と結合する。基体は、結合
が起った位置の特定のために顕微鏡検出装置内に置かれ
る。この顕微鏡検出装置は基体に光を向けるための単色
光源又は多色光源、基体からの蛍光を検出するための手
段、及び蛍光の場所を決定するための手段を含む。
かの態様においては光子カウンターを含むであろう。蛍
光の位置を決定するための手段は基体のためのx/y移
動(translation)を含むであろう。スライ
ドの移動及びデーターの収集は適切にプログラムされた
デジタルコンピューターにより記録されそして受理され
る。本発明の性質及び利点の更なる理解は本明細書の残
りの部分及び添付された図面への言及により実現される
であろう。
びヤギ抗マウスへの暴露 I.YGGFLのモノマー並列形成及びそれに続く標識
された抗体への暴露 J.YGGFL及びPGGFLのモノマー並列合成 K.YGGFL及びYPGGFLのモノマー並列合成 L.16種類の異るアミノ酸配列の並列の合成及びHe
rz抗体に対する相対結合親和性の評価 VIII.具体例の例示 IX.結 論
合、下記の一般的意味を有する。 1.相補的 リガンド分子及びその受容体の相互作用する表面の形態
的(topological)適合性又は一致性に関す
る。すなわち、受容体とそのリガンドは相補的であると
記述することができ、そしてそれ故にその接触表面特性
は相互に相補的である。 2.エピトープ 抗体として知られる受容体のサブクラスとの相互作用領
域により描写される抗原分子の部分。
本発明により研究され得るリガンドの例には、限定的で
はないが、細胞膜受容体に対するアゴニスト及びアンタ
ゴニスト、毒素(toxin及びvenom)、ウイル
スエピトープ、ホルモン(例えば、鎮静剤、あへん剤、
ステロイド等)、ホルモン受容体、ペプチド、酵素、酵
素基質、補因子、薬物、レクチン、糖、オリゴヌクレオ
チド、核酸、オリゴサッカライド、蛋白質、及びモノク
ローナル抗体が含まれる。
のセットの構成質。モノマーのセットは限定的ではない
が例えば通常のL−アミノ酸のセット、D−アミノ酸の
セット、合成アミノ酸のセット、ヌクレオチドのセッ
ト、並びにペントース及びヘキソースのセットが含まれ
る。本明細書において使用する場合、モノマーはポリマ
ーの合成のための基本セットのいずれかの構成員に関す
る。例えば、L−アミノ酸のダイマーはポリペプチドの
合成のための400のモノマーの基本セットを構成す
る。モノマーの異る基本セットはポリマーの合成におけ
る逐次段階で使用されるであろう。
て一緒に結合しているポリマーであって、ポリペプチド
とも称する。この明細書の文脈において、アミノ酸はL
−光学異性体又はD−光学異性体であり得る。ペプチド
は2より多くのアミノ酸モノマーの長さを有し、そして
しばしば20より多くのアミノ酸モノマーの長さを有す
る。アミノ酸のために標準的略号が用いられる(例え
ば、プロリンについてはP)。これらの略号はStry
er,Biochemstry、第3版、1988に含
まれており、これをすべての目的のために引用により本
明細書に組み入れる。
線放射、可視光、赤外線放射、マイクロウエーブ放射及
びラジオ波を包含する10-14 メートル及び104 メー
トルの間の波長を有するエネルギーを含めて、選択的に
適用され得るエネルギー。「照射」とは、表面への放射
の適用を意味する。
天然分子でも人造分子でもよい。さらに、これらはその
変化していない状態で又は他の種との凝集体として用い
ることができる。受容体は共有結合により又は非共有結
合により、直接に又は特定の結合物質を介して結合員に
付加され得る。本発明により使用され得る受容体の例に
は、限定的ではないが、抗体、細胞膜受容体、特定の抗
原決定基(例えばウイルス、細胞又は他の材料上にある
もの)と反応するモノクローナル抗体及び抗血清、薬
物、ポリヌクレオチド、核酸、ペプチド、補因子、レク
チン、糖、ポリサッカライド、細胞、細胞膜、及びオル
ガネラが含まれる。
ンドとも称される。本明細書において受容体なる用語が
使用される場合、意味の相違は意図されない。2つの巨
大分子が分子認識を介して結合して複合体を形成する場
合、「リガンド受容体対」が形成される。本発明により
研究され得る受容体の他の例には次のものが含まれる
が、これらに限定されない。
き、受容体に結合するリガンドの決定は新しいクラスの
抗生物質において有用である。特に価値あるものは、日
和見真菌、原生動物、及び現在使用されている抗生物質
に対して耐性を有する細菌に対する抗生物質であろう。 b)酵 素 例えば、神経伝達物質の開裂を担当する酵素のごとき酵
素の結合部位;異る神経伝達物質を開裂せしめる酵素の
作用を変更するある種の受容体に結合するリガンドの決
定は、神経伝達の不全の治療において使用され得る薬剤
の開発において有用である。
抗体分子上のリガンド結合部位の研究において有用であ
り、抗原性エピトープを模倣する配列の決定はワクチン
の開発を導くことができ、該ワクチンの免疫原は1又は
複数のこの様な配列に基き、あるいは前記決定は療法的
処置において、例えば自己免疫疾患に対して(例えば
「自己」抗体の結合をブロックすることにより)有用な
関連診断剤又は化合物の開発を導くことができる。
することができる。 e)触媒的ポリペプチド 1又は複数の反応体の1又は複数の生成物への転換を含
む化学反応を促進することができるポリマー、好ましく
はポリペプチド。この様なポリペプチドは一般に少なく
とも1つの反応体又は反応中間体に対して特異的な結合
部位、及び該結合部位の近くにある活性官能基を含み、
この官能基は結合した反応体を化学的に変形することが
できる。触媒的ポリペプチドは例えば米国特許出願N
o.404,920に記載されており、これをすべての
目的のため引用により本明細書に組み入れる。
い親和性をもって受容体に結合するリガンドの決定は、
例えば、糖尿病の症状の救済のために糖尿病患者がとら
なければならない日常的注射に代る経口投与の開発、及
び他の場合、死体から又は組換えDNA技法によっての
み得ることができる少ないヒト成長ホルモン代替におい
て有用である。他の例は血管収縮ホルモン受容体であ
り、受容体に結合するリガンドの決定は血圧を制御する
薬剤の開発を導くであろう。 g)オピエート(opiate)受容体 脳におけるあへん受容体に結合するリガンドの決定はモ
ルフィン及び関連薬剤の耽溺性の少ない代替物の開発に
おいて有用である。
ては基体の少なくとも1つの表面は実質的に平らである
が、幾つかの態様においては、異るポリマーのための合
成領域を例えばウエル、隆起した領域、エッチングされ
た溝等により物理的に分離するのが望ましい。他の具体
例に従えば、合成の完了の後に放出される小ビーズを表
面に備えることができる。
ときアクチベーターへの暴露に際して空間的に除去され
る材料。本発明において用途を有する保護基の例にはニ
トロベーラトリルオキシカルボニル(Nitrover
atryloxycarbonyl)、ニトロベンジル
オキシカルボニル、ジメチルジメトキシベンジルオキシ
カルボニル、5−ブロモ−7−ニトロインドリニル、o
−ヒドロキシ−α−メチルシンナモイル、及び2−オキ
シメチレンアンスラキノンが含まれる。アクチベーター
の他の例にはイオンビーム、電界、磁界、電子ビーム、
X−線等が含まれる。
か、活性化されているか、又は活性化されることが意図
される表面上の位置決定された領域である。所定の領域
は任意の便利な形状、例えば円形、長方形、楕円形、く
さび形等を有することができる。本明細書において簡略
化のため、「所定の領域」を時として単に「領域」と称
する。
別する特性を示す場合、ポリマーは所定の領域内で「実
質的に純粋である」と考えられる。典型的には純度は、
均一な配列の結果としての生物学的活性又は機能として
測定されるであろう。この様な特性は典型的には選択さ
れたリガンド又は受容体との結合により測定されるであ
ろう。
する基体の調製及び使用のための方法及び装置を提供す
る。本発明はこの明細書において主として、アミノ酸の
配列を含む分子の製造に関して記載されるが、しかし他
のポリマーの製造にも容易に適用することができる。こ
の様なポリマーには、例えば、核酸の直鎖状及び環状ポ
リマー、ポリサッカライド、リン脂質、α−、β−又は
ω−アミノ酸を有するペプチド、上記のいずれかに既知
の薬物が共有結合しているヘテロポリマー、ポリウレタ
ン、ポリエステル、ポリカーボネート、ポリウレア、ポ
リアミド、ポリエチレンイミン、ポリアリーレンスルフ
ィド、ポリシロキサン、ポリイミド、ポリアセテート、
あるいはこの開示の概観の後に明らかになるであろう他
のポリマーが含まれる。好ましい態様において、本発明
はペプチドの合成に使用される。
合のためのリガンドとして種々のポリマーをスクリーニ
ングするのに使用されるが、しかし本発明はリガンドと
結合する受容体の合成のためにも使用することができ
る。この明細書に開示される基体は、広範な種類の他の
用途を有するであろう。単に例として、本明細書におい
て本発明は蛋白質に結合する核酸配列及びペプチド配列
の決定、配列特異的結合薬剤の発見、抗体により認識さ
れたエピトープの同定、並びに臨床的及び診断的用途並
びに上記の組合わせのための種々の薬剤の評価におい
て、使用され得る。
「S」の使用を提供する。場合によっては基体の表面に
リンカー分子「L」が与えられる。幾つかの態様におい
て、リンカーの目的は合成されたポリマーの受容体認識
を促進することである。場合によっては、リンカー分子
は貯蔵の目的のために化学的に保護されていてもよい。
幾つかの態様においてはt−BOC(t−ブトキシカル
ボニル)のごとき化学的貯蔵保護基を用いることができ
る。この様な化学的保護基は、例えば酸性溶液への暴露
の後に化学的に除去され、そして貯蔵の間に表面を保護
するために役立ちそしてポリマーの調製に先立って除去
されるであろう。
P0 を有する官能基が与えられる。保護基P0 を放射、
電界、電流又は他のアクチベーターへの暴露に際して除
去して官能基を露出させることができる。好ましい態様
において、放射は紫外線(UV)、赤外線(IR)又は
可視光である。後でさらに十分に記載するように、保護
基は、電界の存在下で除去され得る電気化学的に感受性
の基であることもできる。さらに他の態様においては、
脱保護のためにイオンビーム、電子ビーム、等を使用す
ることもできる。
域、そしてそれ故に各異るポリマー配列がその上で合成
される範囲は約1cm2 より小さく又は1mm2 未満であ
る。好ましい態様においては、暴露される範囲は約1
0,000μm2 未満であり、さらに好ましくは100
μm2 未満であり、そして幾つかの態様においては単一
分子と同様に少数のための結合部位を含むことができ
る。これらの領域内で、各ポリマーは好ましくは実質的
に純粋な形で合成される。光への基体の既知領域の暴露
と同時に又はその後に、表面を第一モノマーユニットM
1 と接触させ、このユニットは脱保護段階において露出
された官能基と反応する。第一モノマーは保護基P1 を
含有する。P1 はP0 と同じでもよく又は異っていても
よい。
一領域は次の配列: S−L−M1 −P1 を含んで成り、他方表面の残りの領域は次の配列: S−L−P0 を含んで成る。次に、表面の第二領域(これは第一領域
を含むことができる)を光に暴露し、そして保護基P2
を有する第二モノマーM2 (これはM1 と同一でもよ
く、又は異っていてもよい)と接触せしめる。P2 はP
0 及びP1 と同一でもよく、又は異っていてもよい。こ
の第二サイクルの後、基体の異る領域は次の配列: S−L−M1 −M2 −P2 S−L−M2 −P2 S−L−M1 −P1 及び/又は S−L−P0 の1又は複数を含んで成るであろう。基体が所望の長さ
の所望のポリマーを含有するまで上記の工程を反復す
る。光に暴露される基体の場所及び暴露に続き基体に暴
露される試薬を制御することにより、各配列の場所が知
られるであろう。
除去し、そして場合によっては配列をキャップユニット
Cによりキャップする。この工程が、次の一般式: S−〔L〕−(Mi ) −(Mj ) −(Mk )…(Mx )
−〔C〕 (式中、中カッコ〔 〕は場合によっては存在する基を
示し、そしてMi …Mxはモノマーの任意の配列を示
す)により示される複数のポリマーを持つ表面を有する
基体をもたらす。モノマーの数は広範囲の値にわたるこ
とができるが、しかし好ましい態様においてはそれは2
〜100の範囲であろう。
場所でポリマーは共通のモノマーサブ配列を含むべきで
ある。例えば、第一の場所において配列S−M1 −M2
−M 3 をそして第二の場所において配列S−M4 −M2
−M3 を合成することが望ましいであろう。この工程は
第一の場所の照射をもって開始され、これに続くM1−
Pとの接触が第一場所での配列S−M1 −Pをもたら
す。次に第二場所を照射しそしてM4 −Pと接触させて
第二場所での配列S−M4 −Pを得る。次に、第一場所
及び第二場所の両方を照射し、そしてダイマーM2 −M
3 と接触せしめることにより第一場所における配列S−
M1 −M2 −M3 、及び第二場所における配列S−M4
−M2 −M3 を得る。言うまでもなく、任意の長さのサ
ブ配列を用いることができ、これには2以上の範囲のモ
ノマー、2〜100個のモノマー、2〜20個のモノマ
ー、そして最も好ましくは2〜3個の範囲モノマーが含
まれる。
に1セットのマスクが使用され、そして次に選択的脱保
護のために種々の波長の光が用いられる。例えば、前に
検討した工程において、第一領域をまずマスクを介して
暴露し、そして第一波長の光(例えばIR)への暴露に
際して除去され得る第一保護基P1 を有する第一モノマ
ーと反応せしめる。第二領域をマスクし、そして第二波
長の光(例えばUV)への暴露に際して除去され得る第
二保護基P2 を有する第二モノマーと反応せしめる。こ
の後、脱保護サイクルにおいて基体全体を第一波長の光
及び第二波長の光に交互に暴露することができるから、
合成においてマスクは不必要となる。
リマーは、例えば生物学的活性のスクリーニングを含め
て種々の用途を有するであろう。このようなスクリーニ
ング活動において、配列を含む基体は、標識されていな
いか又は標識されている受容体、例えば抗体、細胞上の
受容体、リン脂質小胞、又は他の種々の受容体のいずれ
かと接触される。1つの好ましい態様においては、ポリ
マーはまず注目の第一の未標識受容体に暴露され、そし
てその後で、例えば抗体である標識された受容体特異的
認識要素に暴露される。この方法は検出段階でのシグナ
ルの増幅をもたらすであろう。
ーと結合することができる。標識された受容体の存在、
そしてそれ故に該受容体と結合する配列の存在が好まし
い態様においてはオートラジオグラフィーの使用、電荷
カップリング(charge−coupled)装置に
よる蛍光の検出、蛍光顕微鏡等により検出される。受容
体の結合が検出される場所におけるポリマーの配列を用
いて該受容体に対して相補的である配列の全部又は部分
を決定することができる。
生物学的活性についてのスクリーニングに言及しながら
説明される。しかしながら、本発明は他の多くの用途を
有する。例えば、本発明は情報の格納(例えば、光ディ
スク上での)、分子電子装置の製造、分離科学(sep
aration sciences)における定常相の
生成、染料及び増白剤の製造、写真、並びに特異的ポリ
マー配列の分子認識を介しての表面上のパターンにおけ
る細胞、蛋白質、レクチン、核酸、ポリサッカライド等
の固定化、において使用することができる。
成することにより、走化性を制御するため又は例えば増
加する量の抗原に対して抗体を力価検定する診断用浸漬
棒(dipstick)を開発するために勾配が確立さ
れるであろう。幾つかの触媒分子を近接して合成するこ
とにより、より効率的な多段階転換によって「座標固定
化」(coordinate immobilizat
ion)が達成され得る。座標固定化はまた、電子伝達
系のため、並びに構造的完全性及び他の好ましい性質、
例えば滑性、湿潤性等を与えるために用いることができ
る。他の態様に従えば、分子生物分配及び薬理速度特性
を試験することができる。例えば、腸プロテアーゼ又は
血清プロテアーゼに対する耐性を評価するため、ポリマ
ーを蛍光タッグによりキャップし、そして注目の生物学
的流体に暴露することができる。
し、ここでは基体2が断面として示される。本質的に、
任意の便利な基体を本発明において使用することができ
る。基体は生物学的、非生物学的、有機、無機、又はこ
れらの任意の組合わせであることができ、粒子、ストラ
ンド、沈澱、ゲル、シート、チューブ、球状体、容器、
毛細管、パッド、スライス、フィルム、プレート、スラ
イド等として存在する。基体は任意の便利な形態、例え
ばディスク、正方形、円等であることができる。
表面構造を取るであろう。例えば、基体はその上で合成
が行われる隆起した又はくぼんだ領域を含むことができ
る。基体及びその表面は好ましくは、本明細書に記載す
る反応がその上で起る硬質の支持体を形成する。基体及
びその表面はまた、適切な吸光特性を与えるように選択
される。
・ブロジェットフィルム(Langmuir Blud
gett)フィルム、官能化されたガラス、Si,G
e,GaAs,GaP,SiO2 ,SiN4 、改質シリ
コン、又は広範囲の種類のゲル又はポリマー、例えば
(ポリ)テトラフルオロエチレン、(ポリ)ビニリデン
ジフルオリド、ポリスチレン、ポリマーボネート、又は
これらの組合せであることができる。他の基体材料はこ
の開示を概観した後に当業者にとって明らかであろう。
好ましい態様において、基体は10Å未満の表面レリー
フ特性を有する単結晶シリコン又は平らなガラスであ
る。幾つかの態様に従えば、基体の表面はよく知られた
方法によりエッチングすることにより所望の表面特性を
与える。例えば、溝、V−形溝、メーサ(台地)構造等
の形成により、合成領域を突き当たる光の焦点内により
密に置くことができ、蛍光源等からの集光の最大化のた
めの反射「鏡」構造を備えることができる。
基体と同じ材料で構成される。すなわち、表面は広範囲
の種類の材料のいずれか、例えばポリマー、プラスチッ
ク、樹脂、ポリサッカライド、シリカもしくはシリカを
基材とする材料、炭素、金属、無機ガラス、膜、あるい
は前に挙げた基体材料のいずれかから構成され得る。幾
つかの態様において、表面は、すでに引用した出願番号
No.404,920の教示に従う基体の表面に堅く結
合したかこまれた(caged)結合員の使用を提供す
る。好ましくは、表面は反応性基を含み、この基はカル
ボキシル、アミノ、ヒドロキシル等であることができ
る。さらに好ましくは、表面は光学的に透明であり、そ
してシリカ表面に見られるように表面Si−OH官能基
を有するであろう。
の層を有するが、リンカー分子は本発明の必須の要素で
はないと理解されよう。リンカー分子は好ましくは、完
成された基体中のポリマーが基体に暴露された分子と自
由に接触することを許容するのに十分な長さを有する。
リンカー分子は十分な暴露を提供するためには6〜50
原子の長さを有すべきである。リンカー分子は例えばア
リールアセチレン、2〜10個のモノマーユニットを含
むエチレングリコールオリゴマー、ジアミン、ジアシ
ド、アミノ酸、又はこれらの組合せであることができ
る。この開示に照らして他のリンカー分子を使用するこ
ともできる。
成されたポリマーの提出を改良するために、リンカー分
子はそれらの親水性/疎水性特性に基いて選択される。
例えば、親水性受容体の場合、該受容体が合成されたポ
リマーに一層密接に接近することを許容するように、親
水性リンカー分子が好ましい。他の態様に従えば、リン
カー分子はまた中間位置に光開裂性基を備える。この光
開裂性基は好ましくは保護基とは異る波長において開裂
される。このことが、異る波長の光への暴露による合成
の完了後の種々のポリマーの取り出しを可能にする。
オロクロロエチレン表面を用いて炭素−炭素結合を介し
て、又は好ましくはシロキサン結合により(例えば、ガ
ラス又は酸化珪素表面を用いて)基体に付加することが
できる。基体の表面とのシロキサンの結合は、1つの態
様においては、トリクロロシリル基を担持するリンカー
分子の反応を介して形成される。リンカー分子は場合に
よっては指定された整列で、すなわち重合されたラング
ミューア・ブロゼットフィルム中のヘッドグループ(h
ead group)の部分として取付けられる。他の
態様においては、リンカー分子は基体の表面に吸着され
る。
びモノマーは、保護基が結合した官能基を備える。好ま
しくは、保護基は基体とは反対側のリンカー分子の遠位
端又は末端に存在する。保護基は負の保護基(すなわ
ち、暴露の後にリンカー分子とモノマーとの反応性を低
くする保護基)又は正の保護基(すなわち、暴露の後に
リンカー分子とモノマーとの反応性を低くする保護基)
のどちらでもよい。負の保護基の場合、反応性化の追加
の段階が必要であろう。幾つかの態様においては、それ
は加熱により行われるであろう。
正の光反応性基から選択することができ、これには好ま
しくはニトロ芳香族化合物、例えばo−ニトロベンジル
誘導体又はベンジルスルホニルが含まれる。好ましい態
様において、6−ニトロベラトリルオキシカルボニル
(NVOC)、2−ニトロベンジルオキシカルボニル
(NBOC)又はα,α−ジメチル−ジメトキシベンジ
ルオキシカルボニル(DDZ)が使用される。1つの態
様においては、ニトロ基に対してオルト位にベンジル性
水素を含有するニトロ芳香族化合物、すなわち、次の
式:
ロ、アリール、アルケニル又は水素であり;R2 はアル
コキシ、アルキル、ハロ、アリール、ニトロ又は水素で
あり;R3 はアルコキシ、アルキル、ハロ、ニトロ、ア
リール又は水素であり;R4はアルコキシ、アルキル、
水素、アリール、ハロ又はニトロであり;そしてR5は
アルキル、アルキニル、シアノ、アルコキシ、水素、ハ
ロ、アリール又はアルケニルである)で表わされる化学
物質が使用される。使用し得る他の物質にはo−ヒドロ
キシ−α−メチルシンナモイル誘導体が含まれる。光除
去可能な保護基は例えばPatchornik,J.Am.Chem.Soc.
(1970) 92:6333及びAmitら、J.Org.Chem. (1974) 3
9:192 に記載されている。これらを引用により本明細
書に組み入れる。
中の試薬との反応のために活性化される。例えば、5−
ブロモ−7−ニトロインドリン基は、カルボニルに結合
する場合、420nmの光への暴露の際に反応する。第二
の態様においては、リンカー分子上の反応性基は、シン
ナメート基を含めて広範囲の種類の負の光反応性基から
選択される。あるいは、反応性基は電子ビームリソグラ
フィー、X−線リソグラフィー、又は他の放射により活
性化又は不活性化される。電子ビームリソグラフィーの
ための適当な反応性基にはスルホニルが含まれる。例え
ば電流源への暴露を含めて他の方法を使用することもで
きる。この開示に照らして他の反応性基及び活性化方法
を使用することもできる。
は、例えば、半導体工業において知られておりそして例
えばSze, VLSI Technology, McGraw-Hill (1983)、及び
Meadら、Introduction to VLSI Systems, Addison-Wesl
ey (1980) (これらをすべての目的のために引用により
本明細書に組み入れる)において知られているタイプの
リソグラフィー技法を用いて、適切なマスク8を介して
光に暴露される。光を、保護基を含む表面に、又は保護
基の除去のために必要とされる光の波長に対して基体が
透過性である限り基体の背後に向けることができる。図
1に示す態様においては、光は保護基を含む基体の表面
に向けられる。図1はこの様なマスク技法の使用を示
し、これらの技法は領域10a及び10b中の連結分子
を活性化しそして官能基を露出させるために正の反応性
基に適用される。
明な材料の層により部分的に被覆された透明な支持体材
料である。不透明材料の部分が除去され、不透明材料は
所望の正確なパターンで支持体表面に残る。図1に示す
ように、マスク8は基体表面と直接に接触され、その上
に投影され、又はそれに近ずけられる。マスクの「開口
部」は、光除去可能な保護基を基体から除去することが
望まれる基体上の場所に対応する。
いて整合を行うことができ、この場合、整合マーク(示
してない)を用いて、事前のパターン化段階を伴うマス
クが次々と正確に重層され、あるいはより複雑な技法が
使用され得る。例えば、Flandersら、「A New Interfer
ometric Alignment Technique 」, App.Phys.Lett. (19
77) 31:426-428(これを引用により本明細書に繰り入れ
る)に記載されている様な干渉(interferom
etric)技法を用いることができる。
するため、幾つかの態様に従えば、マスクと基体との間
のコントラスト増強材料を設けるのが好ましい。このコ
ントラスト増強層は光により分解される分子、例えばキ
ノンジアジド、又は注目の波長において一時的に漂白さ
れる物質を含んで成ることができる。物質の一時的漂白
は、光が当てられた場所でのより大きな貫通を可能に
し、これによりコントラストが増強されるであろう。あ
るいは、コントラストの増強は、クラッド形ファイバー
束(cladded fiber optic bun
dle)により得ることができる。
イオード等からのものであることができる。非平行光源
が使用される場合、基体への光の拡散を防止するため厚
いマスク又は多層マスクを用いるのが好ましい。さら
に、幾つかの態様においては、合成を制御するために異
る波長に対して感受性の基を用いることが望ましい。例
えば、異る波長に対して感受性の基を用いることによ
り、ポリマーの合成における枝位置を選択し又はあるマ
スキング段階を略すことができる。幾つかの反応性基を
その脱保護のための対応する波長と共に表1に示す。
体の選択された領域を照明するためのマスクの使用によ
り説明するが、他の技法を用いることもできる。例え
ば、変調されたレーザー又はダイオード光源のもとで基
体を翻訳することができる。この様な技法は例えば米国
特許No.4,719,615(Feyrerら)に記載され
ており、引用によりこの明細書に繰り入れる。他の態様
においては、レーザーガルバノメータースキャンナーが
用いられる。
書で「光バルブ」と称する)又は光ファイバー光源上で
又はそれらと接触して合成を行うことができる。液晶を
適切に調節する(modulate)ことにより、光が
基体上の選択された領域に接するように光を選択的に制
御することができる。あるいは、光が選択的に当てられ
る一連の光ファイバーの末端で合成を行うことができ
る。光の暴露の場所を制御するための手段は当業者に明
らかであろう。基体は溶液(示してない)と接触して又
は接触しないで照射されることができ、そして好ましく
は溶液と接触して照射される。幾つかの態様に従えば、
この溶液は、照射により生成した副生成物がポリマーの
合成を妨害するのを防止する試薬を含有する。この様な
副生成物には例えば二酸化炭素、ニトロソカルボニル化
合物、スチレン誘導体、インドール誘導体、及びそれら
の光化学反応の生成物が含まれよう。
るための試薬を含有することができる。溶液に添加され
る試薬にはさらに、例えば、酸性もしくは塩基性の緩衝
剤、チオール、置換されたヒドラジン及びヒドロキシル
アミン、還元剤(例えばNADH)、又は所与の官能基
と反応することが知られている試薬(例えば、アリール
ニトロソ+グリオキシル酸→アリールホルムヒドロキサ
メート+CO2 )が含まれる。照射段階と同時に又はそ
の後に、リンカー分子を洗浄し、あるいは図2中の領域
12a及び12bに「A」で示される第一モノマーと接
触せしめる。第二モノマーは、光に暴露された連結分子
の活性化された官能基と反応する。好ましくはアミノ酸
である第一モノマーはまた光保護基を備えている。モノ
マー上の光保護基は連結分子中に用いられた保護基と同
一でも又は異っていてもよく、そして前記の保護基のい
ずれかから選択される。1つの態様においては、Aモノ
マーのための保護基は基NBOC及びNVOCから選択
される。
キング段階において保護されていた領域として示される
領域14a及び14b中のリンカー保護基を除去しそし
て官能基を露出するように位置変えされたマスクを用い
て照射の工程を反復する。第一マスクの位置変えの1つ
の選択肢として、多くの態様において第二マスクが使用
されるであろう。他の態様においては、幾つかの段階が
複数の逐次段階における共通領域の照射をもたらすであ
ろう。図3に示すように、照射された領域間の分離をも
たらすのが望ましい。例えば、整列の許容のためには約
1〜5μmの分離が適当であろう。
護されたモノマー「B」に暴露してB領域16a及び1
6bを生成せしめる。次に、A領域12a及びB領域1
6b上の保護基を除去しそして反応性基を露出するよう
に基体を再びマスクする。基体を再びモノマーBに暴露
し、図6に示す構造の形成をもたらす。ダイマーB−A
及びB−Bが基体上に生成されている。Aについて上に
記載したのと同様の引き続く一連のマスキング及び接触
段階(示してない)が図7に示す構造をもたらす。この
方法は、B及びAのすべての可能なダイマー、すなわち
B−A,A−B,A−A、及びB−Bをもたらす。
ための領域は任意のサイズ及び形状のものでよい。例え
ば、正方形、楕円形、長方形、三角形、円形、又はこれ
らの部分、並びに不規則な幾何学形状を使用することが
できる。冗長性の目的で単一の基体に2連の合成領域を
適用することもできる。1つの態様においては、基体上
の領域12及び16は約1cm2 と10-10cm2との間の表
面積を有するであろう。幾つかの態様においては、領域
12及び16は約10-1 cm2,10-2 cm2,10-3 c
m2,10-4 cm2,10-5 cm2,10-6 cm2,10-7 c
m2,10-8 cm2又は10-10cm2未満の面積を有する。好
ましい態様においては、領域12及び16は10×10
μmと500×500μmとの間である。
0種類より多くのモノマー配列を支持し、そして好まし
くは100種類より多くのモノマー配列を支持してお
り、但し幾つかの態様においては約103 ,104 ,1
05 ,106 ,107 又は10 8 種類より多くの異る配
列が1つの基体に与えられる。言うまでもなく、モノマ
ー配列が合成される基体の1領域内で、モノマー配列が
実質的に純粋であることが好ましい。幾つかの態様にお
いて、基体の領域は少なくとも約1%,5%,10%,
15%,20%,25%,30%,35%,40%,4
5%,50%,60%,70%,80%,90%,95
%,96%,97%,98%又は99%の純度を有す
る。幾つかの態様に従えば、生物学的活性の最初のスク
リーニングを提供するために単一の領域内に意図的に幾
つかの配列をもうけ、次に有意な結合を示す領域内の物
質をさらに評価する。
にポリマーを合成するための反応器系100の好ましい
態様を示す。この反応器系はその表面上に空洞104を
有する体部102を含む。好ましい態様においては空洞
は約50〜1000μmの深さを有し、約500μmの
深さが好ましい。空洞の底には好ましくは隆起106の
整列が設けられており、この隆起はこの図の平面に、及
び図の平面に対して平行に伸びている。隆起は好ましく
は約50〜200μmの深さを有しそして約2〜3mmの
間隔を有する。隆起の目的はより良い混合のために乱流
を生じさせることである。空洞の底部表面は、突き当た
る光の反射を防止するために、好ましくは吸光性であ
る。
る。基体にはその底部表面にそって、介在するリンカー
分子を伴って又は伴わないでNVOCのごとき光除去可
能な保護基が設けられる。この基体は好ましくは広いス
ペクトルの光に対して透過性であるが、しかし幾つかの
態様においては当該保護基を除去する波長に対してのみ
透過性である(例えば、NVOCの場合UV)。幾つか
の態様において、基体は常用の顕微鏡ガラススライド又
はカバースリップである。基体は好ましくは、適当な物
理的支持を提供しながら可能な限り薄いものである。好
ましくは、基体は1mm未満の厚さを有し、さらに好まし
くは0.5mm未満の厚さを有し、さらに好ましくは0.
1mm未満の厚さを有し、そして最も好ましくは0.05
mm未満の厚さを有する。他の好ましい態様においては、
基体は石英又はシリコンである。
を除き空洞を封止するために役立つ。幾つかの態様にお
いては、体部及び基体は1個又は複数個のガスケットに
よって封止のために適合していてもよい。好ましい態様
に従えば、体部は2個の同心ガスケットを有し、そして
介在する空間はガスケットへの基体の適合を確保するた
めに真空状体に維持される。流体は、例えばエルデック
ス・ラボラトリーズ(Eldex Laboratories)により製造
されたモデルNo.B−120−Sでもよいポンプ11
6により前記入口を通して空洞にポンプ輸送される。選
択された流体はポンプにより空洞に入り、該空洞を通過
しそして出口から出て循環され、さらに再循環されるか
又は廃棄される。幾つかの態様においては撹拌を助ける
ため反応器を超音波照射にかけ、及び/又は加熱しても
よい。
られており、このレンズは例えば2インチ100mm焦点
距離の溶融シリカレンズであってもよい。コンパクトな
系のためには、光源124からの光を基体に向けるため
反射鏡122を設けてもよい。光源124は例えば、オ
リエル(Oriel)により製造されそしてモデルN
o.66024を有するXe(Hg)光源であることが
できる。第二レンズ126はレンズ112と組合わされ
てマスクイメージを基体に投影する目的で設けることが
できる。リソグラフィーのこの形態を本明細書において
投影プリンティングと称する。この開示から明らかなよ
うに、幾つかの態様に従えば近接プリンティング(pr
oximity printing)等を用いることも
できる。
て基体の選択された場所にのみ到達することが許され
る。マスク128は例えば、その上にエッチングされた
クロムを有するガラススライドである。1つの態様にお
いてマスク128は透過性場所と不透過性場所の格子を
有する。この様なマスクは例えばフォト・サイエンス社
(Photo Sciences, Inc.)により製造されるであろう。
光はマスクの透明領域を自由に通過するが、しかし他の
領域においては反射されるか又は吸収される。従って、
基体の選択された場合のみが光に暴露される。
するために常用のマスクに代えて光バルブ(LCD)を
用いることができる。あるいは、マスクのコントラスト
の強化の目的で又は光が当てられる領域を限定する唯一
の手段として、ショット・グラス社(Schott Glass, In
c.)から入手できるような光ファイバーフェースプレー
ト(fiber optic faceplate)を
用いることができる。この様なフェースプレートは図8
に示される反応器中の基体上又はそのすぐ上方に置かれ
るであろう。さらに他の態様においてはコントラストの
増強のためにフライスアイ(flys−eys)レン
ズ、テーパー形光ファイバーフェースプレート等を用い
ることができる。
さらに精巧な技法を用いることができる。例えば、好ま
しい態様に従えば、例えばマイクロピペットの先端の分
子マイクロクリスタルにより光が基体に向けられる。こ
の様な装置はLieberman ら「A Light Source Smaller T
han the Optical Wavelength」, Sciene (1990) 247:5
9-61 に記載されており、これをすべての目的のため引
用により本明細書に組み入れる。操作において、基体を
空洞上に置き、そしてそれに対して封止する。基体を調
製する工程のすべての操作は、主として又は全体とし
て、保護基を除去する際の光範囲外の波長の光により照
らされた室内で行われる。例えば、NVOCの場合、U
V光をほとんど又は全く提供しない常用の暗室光により
室が照らされるべきである。すべての操作は、好ましく
はおよそ室温において行われる。
が空洞を通して循環される。この溶液は好ましくはジオ
キサン溶液中5mM硫酸であり、この溶液は露出されたア
ミノ基をプロトン化し続けるために役立ちそして光分解
副生成物とのそれらの反応性を低下させる。この脱保護
流体には、例えば、光を吸収しそして反射及び不所望の
光分解を回避するために役立つN,N−ジエチルアミノ
2,4−ジニトロベンゼンのごとき吸収材料を含めるこ
とができる。
して基体上の第一場所が照明されるようにし、そして次
に脱保護する。好ましい態様においては、基体を約1〜
15分間照明する。好ましい照明時間は365nmの光で
10〜20mW/cm2 にて約10分間である。光分解の
後、例えば塩化メチレン中ジ−イソプロピルエチルアミ
ン(DIEA)の溶液により約5分間スライドを中和す
る(すなわち約7のpHにする)。
置く。照射の後、スライドをはずし、ばらばらに処理
し、そして流れセル中に再設置する。あるいは、好まし
くはやはり保護基により保護されている第一モノマーを
含有する流体をポンプ116により空洞を通して循環さ
せる。例えば、第一場所で基体にアミノ酸Yを結合させ
ることが望まれる場合、アミノ酸Y(そのα−窒素に保
護基を担持する)を、該モノマーを反応性にするために
使用される試薬及び/又はキャリャーと共に貯蔵容器1
18からポンプにより空洞を通って循環させ、そして該
ポンプの入口に戻す。好ましい態様においては、モノマ
ーキャリャー溶液は、第一溶液(本明細書において溶液
「A」と称する)及び第二溶液(本明細書において溶液
「B」と称する)を混合することにより形成する。表2
に溶液Aのために使用し得る混合物の例を示す。
を混合し、そして室温にて約8分間反応せしめ、次に2
mlのDMFにより希釈し、次に500μlをスライドの
表面に適用するか、あるいは該溶液を反応系を通して循
環させ、そして室温にて約2時間反応させる。次にスラ
イドをDMF、塩化メチレン及びエタノールにより洗浄
する。
空洞を通って循環する際、該アミノ酸又は他のモノマー
はそのカルボキシ末端において、脱保護されている基体
の領域上のアミノ基と反応するであろう。言うまでもな
く、本発明を空洞を通してのモノマーの循環を用いて説
明するが、スライドを反応器から取り外しそしてそれを
適切なモノマー溶液に浸漬することによって本発明を実
施することもできる。
ミノ酸を含有する溶液を系から排除する。アミノ酸の除
去が保証される程十分な量(例えば、空洞及びキャリャ
ー管路の容積の約50倍)のDMF/塩化メチレンの循
環の後、マスク又は基体を再配置しあるいは新たなマス
クを使用して基体上の第二領域を光に暴露し、そして光
124を第二の暴露のために用いる。これが基体上の第
二領域を脱保護し、そしてこの方法を目的のポリマー配
列が合成されるまで反復する。次に、誘導体化された基
体全体を、好ましくは例えば蛍光標識により標識された
注目の受容体に暴露する。これは、該受容体の溶液又は
懸濁液を空洞を通して循環させるか、又はスライドの表
面をばらばらに接触せしめることにより行う。受容体
は、相補的配列を含む基体のある領域に優先的に結合す
るであろう。
約1%のBSA(ウシ血清アルブミン)及び0.5%
Tweenの溶液であることができる「スーパーカクテ
ール」と一般に称されるものの中に典型的には懸濁され
る。抗体はスーパーカクテール緩衝液中に例えば約0.
1〜4μg/mlの最終濃度に希釈される。図9は、図8
に示す反応器の他の好ましい態様を示す。この態様に従
えば、マスク128が基体に直接接触して置かれる。好
ましくは、光の分散の効果を減少させるように、マスク
のエッチングした部分を下に向けて配置される。この態
様に従えば、マスクは基体に近接して置かれるので像影
レンズ120及び126は必要でない。
的で、本発明の幾つかの態様は、第一の標識されている
か又は標識されていない受容体への基体の暴露、及びこ
れに続く、該第一受容体上の複数の部位に結合する標識
された第二受容体(例えば抗体)への暴露を用いる。例
えば、第一受容体が第一の種の動物に由来する抗体であ
れば、第二受容体は該第一の種と関連するエピトープに
向けられた第二の種に由来する抗体である。
複数の部位に結合させるために抗−マウスである蛍光標
識されたヤギ抗体又は抗血清を用いて、各結合部位への
単一マウス抗体の結合と比べてて数倍の蛍光を得ること
ができる。更なるシグナルの増幅のため、追加の抗体
(例えば、ヤギ−マウス−ヤギ)を用いてこの方法を反
復することができる。好ましい態様においては、順序付
けられた一連のマスクが使用される。幾つかの態様にお
いては、所与のモノマーセットの可能なポリマーのすべ
てを合成するために1個という少ない数のマスクを使用
することが可能である。
のジヌクレオチドを合成することが望まれる場合、1cm
平方の合成領域が各0.25cm幅の16個の箱に概念的
に分けられる。第一マスクは箱の最左列を暴露し、ここ
ではAが結合する。第二マスクは次の列を暴露し、ここ
ではBが結合され、次にC列のための第三マスクが使用
され、そしてDのために最左列を暴露する最終マスクが
用いられる。第一、第二、第三及び第四マスクは異る場
所に移動される単一マスクであることができる。
は水平方向に反復される。この時、マスクはやはり0.
25cm幅の水平行の暴露を可能にする。反応領域の水平
の4分の1を暴露するマスクを用いてA,B,C及びD
が逐次結合される。得られる基体は4塩基の16種のダ
イマーすべてを含有する。ジペプチドを含有するために
用いられる8個のマスクは移動、又は回転により相互に
関連している。実際に、それが適切に移動又は回転され
れば1個のマスクを使用することができる。例えば、単
1の透明領域を有するマスクを逐次使用して垂直列のそ
れぞれを暴露し、90°移動させ、そして次に水平行の
暴露のために逐次使用することができる。
類の異るモノマー、第二レベルにおいて4種類の異るモ
ノマー、及びストリップパターンの第三レベルにおける
5種類の異るモノマーを有する3モノマー(残基)のポ
リマー鎖の合成のための、それぞれのマスクプログラム
及びサンプルアウトプットの計画のためのQuickB
asicの単純なコンピュータープログラムを提供す
る。プログラムのアウトプットは、セルの数、各マスク
上の「strips」(光領域)の数、及びマスクの各
暴露のために必要な移動の量である。
の蛍光検出装置を示す。基体112はx/y移動テーブ
ル202の上に置かれる。好ましい態様においては、x
/y移動テーブルはニューポート社(New port Corpora
tion)により製造されるモデルNo.PM500−A1
である。x/y移動テーブルは、例えば適切にプログラ
ムされたIBM PC/AT又はAT適合コンピュータ
ーであってもよい適切にプログラムされたデジタルコン
ピューター204に接続されそしてそれにより制御され
る。
するATコンピューターに代えて他のコンピューター
系、特定の目的のハードウエアー等を容易に用いること
もできる。本明細書に記載する移動及びデーター収集機
能のためのコンピューターソフトウエアーは、例えばナ
ショナル・インストルメンツ(National Instruments)
によりライセンスされる「Lab Windows」
(すべての目的のため引用により本明細書に組み入れ
る)を含めて、市販のソフトフエアーに基いて提供され
得る。
数の対物レンズ208を含む顕微鏡206のもとに置か
れる。幾つかの態様においてはスペクトロフィジックス
(Spectraphysics)により製造されるモデルNo.20
20−05アルゴンイオンレーザーであるレーザー21
0からの光(約488nm)が、約520nmより長い波長
の光を通すがしかし488nmの光を反射するダイクロイ
ックミラー(dichroicmirror)207に
より基体に向けられる。ダイクロイックミラー207は
例えばカール・ザイス(Carl Zeiss)により製造される
モデルNo.FT510である。次にこのミラーから反
射された光は顕微鏡206に入り、この顕微鏡は例えば
カール・ザイスにより製造されるモデルNo.Axio
scop20であることができる。基体上のフルオレッ
セインでマスクされた物質は>488nmの光で蛍光を発
し、そしてこの蛍光は顕微鏡により集められ、そして鏡
を通過するであろう。
09を通りそして次に開口板211を通るように向けら
れる。波長フィルター209は例えばメレス・グリオッ
ト(Melles Griot)により製造されるモデルNo.OG
530であることができ、そして開口板211は例えば
カール・ザイスにより製造されるモデルNo.4773
52/477380であることができる。次に蛍光は、
幾つかの態様においてはハママツにより製造されるモデ
ルNo.R943−02である光増倍管212に入り、
シグナルは前増幅器214において増幅され、そして光
子が光子カウンター216によりカウントされる。光子
の数はコンピューター204において場所の関数として
記録される。
ド・リサーチ・システムスにより製造されるモデルN
o.SR440であることができ、そして光子カウンタ
ーはスタンホード・リサーチ・システムスにより製造さ
れるモデルSR400であることができる。次に、基体
を次の場所に移かし、そして工程を反復する。好ましい
態様においては、データーは1〜100μmごとに得ら
れ、約0.8〜10μmのデーター収集直径が好まし
い。十分に高い蛍光を示す態様において、広視野照明を
用いるCCD検出器が用いられる。
電子の数をカウントすることにより、蛍光標識された分
子が位置する基体上の場所を決定することができる。次
に、例えばその表面上に合成されたポリペプチドのマト
リクスを有するスライドについて、ポリペプチドのどれ
が蛍光標識された受容体に対して相補的であるかを決定
することができる。
光の強度及び時間は、蛍光放射を最大にしそしてバック
グラウンドノイズを最小にすることによるシグナル対ノ
イズ比の改善のために、レーザー出力及びスキャンステ
ージ速度を変えることにより調節される。検出装置を、
本明細書においては主として、標識された受容体の検出
に関して説明したが、本発明は他の分野でも用途を有す
るであろう。例えば、本明細書において開示される検出
装置は触媒、DNA又は蛋白質のゲルスキャンニング等
の分野において使用することができるであろう。
対する受容体の存在又は不存在が検出され得るのみなら
ず、種々の配列に対する受容体の相対的結合親和性を決
定することができる。実際に、受容体は整列している幾
つかのペプチド配列に結合するが、幾つかの配列には他
の配列に対するよりも強く結合することが見出される。
多くの受容体分子が強く結合したリガンドの領域中で結
合するであろうから、強い結合親和性は強い蛍光又はラ
ジオグラフィーシグナルにより証明されるであろう。
するリガンドを有する基体の特定の領域においては比較
的小数の受容体分子が結合するため、弱い結合親和性は
弱い蛍光又はラジオグラフィーシグナルによって証明さ
れるであろう。従って、リガンドの相対結合アビディテ
ィ(avidity)(又は、1価相互作用の場合には
親和性)を、該リガンドを含有する領域の蛍光又はラジ
オグラフィーシグナルの強度によって決定することが可
能になる。親和性についての半定量的データーもまた洗
浄条件及び受容体の濃度を変えることにより得られるで
あろう。これは、例えば、既知のリガンド受容体対と比
較することにより行われるであろう。
すべての操作は、特にことわらない限りおよそ周囲温度
及び圧力において行われた。 A.スライドの調製 反応性基の結合の前に、好ましい態様においては顕微鏡
スライド又はカバースリットのごときガラス製基体であ
る基体を清浄にするのが好ましい。1つの態様に従え
ば、例えば120mlの水及び120gの水酸化ナトリウ
ムを含む95%エタノール1lから成るアルカリ浴にス
ライドを12時間浸漬する。次にスライドを流水で洗浄
しそして空気乾燥し、そして95%エタノールの溶液で
一度すすぐ。
ノ基を付加する目的で、スライドを例えばアミノプロピ
ルトリエトキシシランによりアミノ化する。しかし、こ
の目的のためにオメガー官能化シランを用いることもで
きる。1つの態様においては0.1%のアミノプロピル
トリエトキシシランが用いられるが、10-7%〜10%
濃度の溶液を使用することができ、約10-3%〜2%が
好ましい。0.1%混合物は、100mlの95%エタノ
ール/5%水混合物に100マイクロリッター(μl)
のアミノプロピルトリエトキシシランを加えることによ
り調製される。この混合物をおよそ周囲温度にてロータ
リーシェーカー上で約5分間撹拌する。次に、500μ
lのこの混合物を各洗浄されたスライドの一方の側の表
面に適用する。スライドをこの溶液からデカントし、そ
して例えば100%エタノールに浸すことにより3回す
すぐ。
120℃の真空オーブンに約20分間入れ、そして次に
室温にて約12時間アルゴン雰囲気中で硬化させる。次
に、スライドをDMF(ジメチルホルムアミド)溶液に
浸し、次に塩化メチレンにより十分に洗浄する。次に、
各アミノ基にNVOC−GABAを結合させるため、ス
ライドのアミノ化された表面を、例えばDMF中NVO
C−GABA(γ−アミノ酪酸)NFS(N−ヒドロキ
シサクシンイミド)の30mM溶液約500μlに暴露す
る。表面を、例えばDMF、塩化メチレン及びエタノー
ルで洗浄する。
ラン…すなわちNVOC−GABAが結合しなかったア
ミノ基…を、無水酢酸とピリジンとの1:3混合物に1
時間暴露することによりアセチル基によりキャップする
(更なる反応を防止するため)。この残留キャッピング
機能を行うことができる他の物質には無水トリフルオロ
酢酸、蟻酸酢酸無水物、又は他の反応性アシル化剤が含
まれる。最後に、スライドをDMF、塩化メチレン及び
エタノールにより再度洗浄する。
合成 図11は、2−モノマーセット:Gly及びPhe(そ
れぞれ、「A」及び「B」により示す)の8種のトリマ
ーの可能な合成を示す。6−ニトロベラトリルオキシカ
ルボキサミド(NVOC−NH)残基で終るシラン基を
担持するガラススライドを基体として調製する。アミノ
基においてNVOCにより保護されたgly及びphe
の活性エステル(ペンタフルオロフェニル、OBt等を
試薬として調製する。この例には関係ないが、モノマー
セットのために側鎖保護基が必要な場合、これらは主鎖
を保護するために使用される光の波長において光反応性
であってはならない。
lのすべての可能な配列を合成するためにはn×lサイ
クルが必要である。1つのサイクルは次のことから成
る: 1.次の残基が付加されるべき部位でのアミノ基の露出
のための適当なマスクを通しての照射、及び脱保護の副
生成物を除去するための適切な洗浄。 2.段階1において特定された部位においてのみ反応す
るであろう単一の活性化されそして保護された(同じ光
化学的に除去可能な基による)モノマーの添加、及び過
剰の試薬を表面から除去するために適当な洗浄。
基体上の各場所が1つの残基により延長されるまでモノ
マーセットの各構成員について反復される。他の態様に
おいては、次の場所への移行の前に幾つかの残基が1つ
の場所において次々と付加される。サイクル時間は一般
にカップリング反応速度により制限され、今や自動化さ
れたペプチド合成においては20分間と短い。場合によ
ってはこの段階の後に、後剤の試薬のために整列を安定
化するために保護基の付加を行う。ポリマーの幾つかの
タイプ(例えばポリマー)のため、全表面の最終的脱保
護(光保護側鎖基の除去)が必要かも知れない。
に、ガラス20は領域22,24,26,28,30,
32,34及び36を備える。図11のBに示すように
領域30,32,34及び36をマスクし、そしてガラ
スを照射し、そして「A」(例えばgly)を含有する
試薬に暴露し、図11のCに示す構造を得る。次に領域
22,24,26及び28をマスクし、ガラスを照射し
(図11のDに示すように)、そして「B」(例えばp
he)を含有する試薬に暴露して図11のEに示す構造
を得る。図11のMに示される構造が得られるまで、示
されるようにセクションを次々にマスク及び暴露して工
程を進行させる。ガラスを照射し、そして場合によって
はアセチル化により末端基をキャップする。示されるよ
うに、gly/pheのすべての可能なトリマーが得ら
れる。
でない。所望により、エタンジチオール及びトリフルオ
ロ酢酸による処理によって側鎖の脱保護を行うことがで
きる。一般に特定のポリマー鎖を得るのに必要な段階の
数は、 n×l (1) により定義され、ここでn=モノマーのベースセット中
のモノマーの数、及びl=ポリマー鎖中のモノマーユニ
ットの数、である。他方、長さlの配列の合成される数
は、 nt (2) である。
有するポリマーの合成を含むであろうマスク法を用いる
ことにより、一層大きな多様性が得られる。極端な例に
おいて、lより短いか又はそれと同じ長さを有するすべ
てのポリマーが合成されれば、合成されるポリマーの数
は: nt +nt-1 +…+n1 (3) であろう。必要とされるリソグラフィー段階の最大数は
一般に、モノマーの各「層」についてnであろう。すな
わち、必要とされるマスクの総数(そして、それ故にリ
ソグラフィー段階の数)はn×lであろう。透過性マス
ク領域のサイズは合成のために利用され得る基体の面積
及び形成されるべき配列の数に依存するであろう。
り、そしてSはこの全面積において望まれる配列の数で
ある。本明細書に開示されるフォトリソグラフィー技法
を用いて、1つの基体上で数千又は数百万のオリゴマー
を同時に製造するために前記の方法を容易に用い得るこ
とを、当業者は理解するであろう。従って、この方法
は、多数の例えばジ−、トリ−、テトラ−、ペンタ−、
ヘキサ−、ヘプタ−もしくはオクタペプチド、又はより
大きなペプチド(又は、対応してポリヌクレオチド)を
特に試験するための可能性をもたらすであろう。
ている。言うまでもなく、自動化法又は半自動化法を用
いることもできよう。試薬の自動添加及び除去によっ
て、必要とする試薬の容量を最小にしそして反応条件を
より注意深く調節するために、基体を流れセル中に配置
することができる。次々に用いるマスクは手動的又は自
動的に適用することができる。
ーの合成 アミノプロピル基及び蛍光基のダイマーの合成におい
て、基体として官能化されたドラポア(durapor
e)膜を用いた。ドラポア(durapore)膜はア
ミノプロピル基を有するポリビニリデンジフルオリドで
ある。アミノプロピル基を、カルボニルクロリドとアミ
ノ酸との反応によりDDZ基によって保護した。この反
応は当業者によく知られた反応である。
に入れ、そして1mmの不透明領域及び透明領域のチェッ
カーボードパターンを有するマスクに接触させた。マス
クを約280nm以上の波長を有する紫外線に5分間、室
温にて暴露した。但し、本発明の種々の態様において、
広範囲の暴露時間及び温度を使用するのが適当である。
例えば、1つの態様においては、−70℃〜+50℃の
工程温度において約1〜5000秒の暴露時間を用いる
ことができる。1つの好ましい態様において、およそ周
囲圧力における約1〜500秒間の暴露時間が使用され
る。幾つかの好ましい態様においては、蒸発を防止する
ために周囲圧より高い圧が用いられる。
キレートに結合した活性エステルを含む蛍光標識により
洗浄した。洗浄時間は数分間〜数時間の広い範囲で異る
であろう。これらの物質は赤及び緑可視領域で蛍光を発
する。フルオロポーア(fluorophore)中活
性エステルとの反応が完了した後、フルオロポーアが結
合した位置を、それらを紫外線に暴露しそして、赤及び
緑の蛍光を観察することにより、可視化することができ
る。基体の誘導体化された領域はマスクのもとのパター
ンに密接に対応することが観察された。
タンダーダ(Flow Cytometry Standard)により製造され
たモデルNo.824の低レベル標準蛍光ビーズキット
を用いて証明された。このキットは、既知の数の蛍光分
子が含浸された直径5.8μmのビーズを含む。
れたレーザーのフィールド中の図10に示すスキャンス
テージ上の証明フィールド中に置いた。証明フィールド
中に置いた後、光子検出装置を作働させた。レーザービ
ームはブロックされず、そして粒子ビームと相互作用
し、これは次に蛍光を発した。7,000及び29,0
00のフルオレッセイン分子で含浸されたビーズの蛍光
曲線をそれぞれ図12及び図13に示す。各曲線上に、
フルオレッセイン分子を伴わないビーズについての追跡
線も示してある。これらの実験は488nmの励起、10
0μWのレーザー出力を用いて行われた。光は40パワ
ー0.75NA対物レンズを通して焦点を結ばせた。
り、そして次に指数的に減少した。強度の低下はフルオ
レッセイン分子の光漂白(photobleachin
g)によるものである。フルオレッセイン分子を伴わな
いビーズの追跡線はバックグラウンドの差引のために用
いられる。標識されたビーズ及び非標識ビーズの間の最
初の指数的低下の差を積分して光子カウントの全数を
得、そしてこの数はビーズ当りの分子の数に関連する。
従って、検出され得るフルオレッセイン分子当り光子の
数を推定することができる。図12及び13に示す曲線
について、この計算が示すところによれば、この計算は
フルオレッセイン分子当り約40〜50個の光子の放射
を示す。
顕微鏡スライドを用いて該スライドの標識化密度を確立
した。スライドの遊離アミノ末端を、該アミノ基と共有
結合を形成するFITC(フルオレッセインイソチオシ
アネート)と反応せしめた。次に、スライドをスキャン
ニングして、フルオレッセント分子当り光子の予想値を
用いて、単位面積当り表面上の分子の数の計算を可能に
する領域中に発生するフルオレッセント光子の数をカウ
ントする。
スライドをDMF中FITCの1mM溶液におよそ周囲温
度にて1時間すすいだ。反応の後、スライドをDMFで
2回、そして次にエタノール、水、そして次に再度エタ
ノールにより洗浄した。次に、それを乾燥し、そしてそ
れが試験され得る状態になるまで貯蔵する。図12及び
13に示すのと同様な曲線を使用し、そして指数的減少
シグナルのもとでの蛍光カウントを積分することによっ
て、誘導体化後の表面上の遊離アミノ基の数を決定し
た。103 ×103 〜約2×2nm当り1フルオレッセイ
ンの標識化密度を有するスライドは、アミノプロピルト
リエトキシシランの濃度が10 -5%〜10-1%の間で異
る間に、再現性よく作ることができ決定された。
のスライドの全表面を光に暴露してγ−アミノ酪酸の末
端の遊離アミノ基を露出した。次に、このスライド及び
暴露されていない同じものをフルオレッセインイソチオ
シアネート(FITC)に暴露した。図14は光に暴露
されなかったがしかしFITCに暴露されたスライドを
示す。X軸の単位は時間であり、Y軸の単位はカウント
である。追跡線はある量のバックグラウンド蛍光を含有
する。もう一方のスライドを350nm広バンド照明に約
1分間暴露し(12mW/cm2 ,〜350nm照明)、洗浄
し、そしてFITCと反応させた。このスライドの蛍光
曲線を図15に示す。蛍光レベルの大きな増加が観察さ
れ、これは、光分解がスライドの表面上の多数のアミノ
基を蛍光マーカーの付加のために露出したことを示して
いる。
行った。Hg−Xeアーク灯からの光を、レーザー切除
したガラス上クロムマスクを通して、基体を直接接触さ
せることにより基体上に像形成した。このスライドを1
2mWの350nm広バンド光により約5分間照明しそして
次に1mM FITC溶液と反応させた。これをレーザー
検出スキャンニングステージ上に置き、そして蛍光強度
のポジションカラーコードの2元表示としてグラフをプ
ロットした。種々のマスクを通して実験を多数回反復し
た。100×100μmマスク、50μmマスク、20
μmマスク及び10μmマスクの蛍光パターンが示すと
ころによれば、このリソグラフィー技法を用いてマスク
パターンは少なくとも約10μm以上で区別される。
Herz抗体及びヤギ抗マウスへの暴露 特定のポリペプチド配列に対する受容体が表面結合ペプ
チドに結合しそして検出されることを確立するために、
Leuエンケファリンを表面に結合させそして抗体によ
り認識させた。スライドを0.1%アミノプロピル−ト
リエトキシシランにより誘導体化し、そしてNVOCに
より保護した。裏側接触印刷(backside co
ntact printing)を用いて流れセル中の
スライドを暴露するため500μmチェッカーボードを
用いた。
シン、グリシン、フェニルアラニン、ロイシン−COO
H、あるいは本明細書においてYGGFLと称する)を
そのカルボキシ末端を介して、スライドの表面上の露出
されたアミノ基に結合させた。ペプチドをBOP/HO
BT/DIEAカップリング試薬と共にDMF溶液に加
え、そして流れセルを通して2時間、室温にて再循環さ
せた。Herz抗体として知られる第一抗体をスライド
の表面に45分間、2μg/mにて、スーパーカクテイ
ル(この場合さらに1%BSA及び1%オバルブミンを
含有する)中で適用した。次に、第二抗体、すなわちヤ
ギ抗−マウス・フルオレッセイン複合体を2μg/mlで
スーパーカクテイル緩衝液中に加え、そして2時間イン
キュベートした。
としてプロットした。この像を10μm段階でとり、そ
して次のことが示された。よく定義されたパターンで脱
保護が行われ得るのみならず、(1)この方法は基体の
表面へのペプチドの好結果のカップリングをもたらし、
(2)結合したペプチドの表面は抗体との結合のために
利用可能であり、そして(3)検出装置の能力は受容体
の結合を検出するのに十分であった。
れに続く標識抗体への暴露 交互の正方形におけるYGGFL及びGGFLのモノマ
ー並列合成をスライド上チェッカーボードパターン中で
行い、そして得られるスライドをHerz抗体に暴露し
た。この実験を図16及び図17に示す。図16におい
て、この場合はt−BOC(t−ブトキシカルボニル)
で保護されているアミノプロピル基により誘導体化され
たスライドを示す。スライドをTFAで処理してt−B
OC保護基を除去した。次に、そのアミノ基においてt
−BOC保護されているE−アミノカプロン酸をアミノ
プロピル基に連結した。アミノカプロン酸はアミノプロ
ピル基と合成されるべきペプチドとの間のスペーサーと
して機能する。
てNVOC−ロイシンに連結した。次に、スライド全体
を12mWの325nm広バンド照明により照明した。次
に、スライドをNVOC−フェニルアラニンと連結しそ
して洗浄した。スライド全体を再び照明し、そして次に
NVOC−グリシンに連結しそして洗浄した。スライド
を再び照明し、そしてNVOC−グリシンに連結して図
16の最後の部分に示す配列を形成した。
互の領域を500×500μmチェッカーボードマスク
を用いる投影プリントを用いて照明し、こうしてグリシ
ンのアミノ基を照明された領域においてのみ露出させ
た。次の連結化学反応段階を行うときNVOC−チロシ
ンを加え、そしてそれを照明を受けた所においてのみ連
結させた。次に、スライド全体を照明してすべてのNV
OC基を除去し、照明された領域にYGGFLのチェッ
カーボードを残し、そして他の領域にGGFLを残し
た。Herz抗体(これはYGGFLを認識するがしか
しGGFLを認識しない)を加え、次にヤギ抗−マウス
・フルオレッセイン結合体を加えた。
より認識されない(そしてそれ故ヤギ抗−マウス抗体・
フルオレッセイン結合体との結合が存在しない)テトラ
ペプチドGGFLを含む領域、及びYGGFLが存在す
る赤い領域を示した。YGGFLペンタペプチドはHe
rz抗体により認識され、そしてそれ故に、照明された
領域にはフルオレッセイン−結合ヤギ抗−マウスが認識
する抗体が存在する。基体との直接接触(「近接プリン
ト」)において使用された50μmマスクについての類
似のパターンはより明瞭なパターンを与え、そしてチェ
ッカーボードパターンの角は、マスクが基体に直接接触
して置かれた結果として感動的であった(これは、この
技法を用いての解像度の増加を反映している)。
並列合成 図16及び17に示したものに類似する50μmチェッ
カーボードマスクを用いての合成を行った。しかしなが
ら、追加の連結段階を通して基体上のGGFL部位にP
を加えた。保護されたGGFLをマスクを通して光に暴
露し、そして次に、前記のようにしてPに暴露すること
によりPを付加した。従って、基体上の領域の半分はY
GGFLを含有し、そして残りの半分はPGGFLを含
有した。この実験についての蛍光プロットが示すところ
によれば、領域はやはり、結合が起った領域と結合が起
らなかった領域との間が容易に識別できる。この実験
は、抗体が特定の配列を認識し得ること、及びこの認識
が長さ依存的でないことを示した。
ー並列合成 本発明の機能可能性をさらに示すため、前記のような技
法を用いて基体上に交互のYGGFL及びYPGGFL
の50μmチェッカーボードパターンを合成した。得ら
れる蛍光プロットが示すところによれば、抗体はYGG
FL配列を明瞭に認識することができそしてYPGGF
L領域には有意に結合しなかった。
合成及びHerz抗体への相対結合親和性の評価 前記の技法に類似する技法を用いて、一連の16種類の
異るアミノ酸配列(4連反復)を2枚のガラス基体のそ
れぞれの上で合成した。スライドの全表面にわたって配
列NVOC−GFLを付加することにより配列を合成し
た。次に、一連のマスクを用いて2層のアミノ酸を基体
に選択的に適用した。各領域は0.25cm×0.062
5cmの寸法を有していた。
アミノ酸配列を含んでおり、そして第二のスライドは選
択されたD−アミノ酸のみを含んだ。図18のA及び図
18のBはそれぞれ第一スライド及び第二スライド上の
種々の領域のマップを示す。図18のA及び図18のB
に示されるパターンは各スライド上に4連反復させた。
次に、スライドをHerz抗体及びフルオレッセイン−
標識ヤギ抗−マウスに暴露した。
の蛍光プロットは赤い領域(強い結合、すなわち14
9,000カウント以上)、及び黒い領域(Herz抗
体がほとんど又は全く結合しない、すなわち20,00
0カウント以下)を示した。配列YGGFLは明らかに
最も強く認識された。配列YAGFL及びYSGFLも
また抗体の強い認識を示した。これに対して、残りの配
列のほとんどが、ほとんど又は全く結合を示さなかっ
た。スライドの4連の反復部分はそこに示される結合の
量において非常に一貫していた。
すところによれば、YGGFL配列により最も強い結合
が示された。YaGFL,YsGFL及びYpGFLに
対しても有意な結合が検出された。残りの配列は抗体と
の低い結合を示した。配列yGGFLの低い結合効率が
観察された。表6は試験された種々の配列を相対蛍光の
順に挙げている。これは相対結合親和性に関する情報を
提供する。
れた(caged)結合員の結合を提供し、この結合員
はその囲まれた形態において、他の潜在的に結合する
種、例えば受容体及び特異的結合基質に対する比較的低
い親和性を有する。この様な技法は、1989年9月8
日出願の係続中の出願No.404,920にさらに十
分に記載されており、これをすべての目的のため引用に
より本明細書に組み入れる。
表面上の所定の領域を形成する方法を提供し、ここで、
所定の領域は受容体を固定化することができる。この方
法は、表面に結合された囲まれた結合員を使用し、所定
の領域の選択的活性化を可能にする。囲まれた結合員
は、所望の領域の選択的活性化の際に遊離されて最終的
に受容体と結合することができる結合員として機能す
る。次に、活性化された結合剤を用いて受容体のごとき
特定の分子を基体の所定の領域に固定化する。上記の方
法を基体上の同一の又は異る部位において反復し、例え
ば同一の又は異る受容体を含有する表面上の複数の領域
を有する表面を得る。こうして固定化された受容体が1
又は複数のリガンドについて異る親和性を有する場合、
そのリガンドについてのスクリーニング及び測定を前記
受容体を含有する表面の領域において行うことができ
る。
た結合員を用いることができる。囲まれた(不活性化さ
れた)構成員は、活性化された結合員の対応する親和性
と比較した場合、囲まれていない結合員に特異的に結合
する物質の受容体に対する比較的低い親和性を有する。
従って、活性化されるべき表面の領域に適当なエネルギ
ー源が適用されるまで、結合員は反応から保護される。
適当なエネルギー源の適用の際、囲んでいる(cagi
ng)基が不安定化し、これにより活性化された結合員
を提出する。典型的なエネルギー源は光である。
れらは受容体に付加され得る。選択される受容体はモノ
クローナル抗体、核酸配列、薬物受容体等であることが
できる。受容体は常にではないが通常、それを直接的又
は間接的に結合員に付加することが可能なように調製す
ることができる。例えば、結合員に対する強い結合親和
性及び受容体又は受容体の結合体(conjugat
e)に対する強い親和性を有する特異的結合物質を用い
て、所望により結合員と受容体との間の架橋として機能
させることができる。この方法は、受容体が特定のリガ
ンドに対するその活性を維持するように調製された受容
体を用いる。
れた結合員は光活性化可能なビオチン複合体、すなわ
ち、アビジン又はアビジン類似体に対して天然ビオチン
に比べて有意に低下した結合親和性を有するように光活
性化可能な保護基により化学修飾されているビオチン分
子であろう。好ましい態様においては、表面の所定の領
域に配置された保護基が適当な放射源の適用の際に除去
されて結合員をもたらし、この結合員はビオチン、又は
アビジンもしくはアビジン類似体に対してビオチンと実
質的に同じ結合親和性を有する機能的に類似する化合物
である。
はアビジン類似体が表面上の活性化された結合員と共
に、該アビジンが該結合員に強く結合するまでインキュ
ベートする。次に、表面の所定の領域上に固定化された
アビジンを所望の受容体又は所望の受容体の結合体と主
にインキュベートすることができる。アビジンが表面の
所定の領域上に固定化される場合、受容体は好ましくは
ビオチン化され、例えばビオチン化抗体であろう。ある
いは、好ましい態様は、あらかじめ調製されたアビジン
/ビオチン化受容体複合体は、表面上の活性化された結
合員に与える。
良された方法及び装置に関する。前記の記載は例示的な
ものであって制限的なものではないことが意図される。
前記の記載を概観した後、当業者には多くの態様が自明
であろう。例として、本発明は主として光除去可能な保
護基の使用に言及して記載しているが、光以外の他の放
射源を使用し得ることが当業者に容易に認識されるであ
ろう。例えば、幾つかの態様において、電子ビーム照
射、X−線照射(電子ビームリソグラフとの組合せにお
ける)、又はX−線リソグラフィー技法に対して選択的
である保護基を用いるのが望ましいであろう。あるい
は、電流への暴露により基を除去することができよう。
従って本発明の範囲は、前記の記載によって決定される
べきではなく、添付された請求の範囲及び該請求の範囲
に均等な全範囲に関して決定されるべきである。
射を示す図である。基体は断面として示される。
図である。
である。
図である。
である。
めの反応器系のいずれか選択可能な具体例を示す図であ
る。
めの反応器系のいずれか選択可能な具体例を示す図であ
る。
るための検出装置を示す図である。
マーの製造に適用される場合の方法を示す図である。
追跡線を示す図である。
追跡線を示す図である。
NVOCスライド及び光に暴露されたNVOCスライド
についての蛍光線を示すグラフである。
NVOCスライド及び光に暴露されたNVOCスライド
についての蛍光線を示すグラフである。
れたYGGFL及びGGFLのチェッカーボードパター
ンを有するスライドの形成を示す図である。
れたYGGFL及びGGFLのチェッカーボードパター
ンを有するスライドの形成を示す図である。
成された16の配列のマッピングを示す図である。
Claims (24)
- 【請求項1】 受容体との結合について複数のアミノ酸
配列をスクリーニングする方法であって、 a)少なくとも第一表面(該少なくとも第一表面はニト
ロベラトリルオキシカルボニル及びニトロベンジルオキ
シカルボニルから成る群から選択された光保護材料を含
んで成る)を有するガラス板上で、前記少なくとも第一
表面を貯蔵のためにt−ブトキシカルボニルと反応せし
め、前記ガラス板は少なくとも紫外光に対して実質的に
透過性である; b)前記少なくとも第一表面をTFAに暴露することに
より前記t−ブトキシカルボニルを除去する; c)前記ガラス板を反応器上に置き、該反応器は反応空
間を含んで成り、前記少なくとも第一表面が該反応空間
に暴露される; d)前記ガラス板上の第一位置にマスクを置き、該マス
クは第一場所及び第二場所を含んで成り、該第一場所は
少なくとも紫外光に対して実質的に透過性でありそして
該第二場所は少なくとも紫外線に対して実質的に不透過
性であり、該第二場所は前記マスクの第一表面上の光遮
断材料を含んで成り、該マスクの該第一表面は前記ガラ
ス板と接触する; e)前記反応空間を反応溶液で充たす; f)前記マスクを少なくとも紫外光により照明し、該紫
外光が前記マスクの前記第一場所下で前記ガラス板の前
記少なくとも第一表面から前記光保護材料を除去する; g)前記第一表面を第一アミノ酸に暴露し、該第一アミ
ノ酸は該少なくとも第一表面の前記光保護材料が除去さ
れた領域に結合し、該第一アミノ酸はその末端に前記光
保護基を含んで成る; h)マスクを前記ガラス板と第二位置において接触せし
める; i)前記マスクを少なくとも紫外光により照明し、該紫
外光が前記マスクの第一場所下で前記ガラス板の前記少
なくとも第一表面から前記光保護材料を除去する; j)前記少なくとも第一表面を第二アミノ酸に暴露し、
該第二アミノ酸は該少なくとも第一表面の前記光保護材
料が除去された領域に結合し、該第二アミノ酸はその末
端に前記光保護基を含んで成る; k)マスクを前記ガラス板と第三位置において接触せし
める; l)前記マスクを少なくとも紫外光により照明し、該紫
外光が前記マスクの前記第一場所下で前記ガラス板の前
記少なくとも第一表面から前記光保護材料を除去する; m)前記少なくとも第一表面を第三アミノ酸に暴露し、
該第三アミノ酸は該少なくとも第一表面の前記光保護材
料が除去された領域に結合する; n)マスクを前記ガラス板と第四位置において接触せし
める; o)前記マスクを少なくとも紫外線により照明し、該紫
外線が前記マスクの前記第一場所下で前記ガラス板の前
記少なくとも第一表面から前記光保護材料を除去する; p)前記少なくとも第一表面を第四アミノ酸に暴露し、
該第四アミノ酸は該少なくとも第一表面の前記光保護材
料が除去された領域に結合し、該少なくとも第一表面は
少なくとも第一、第二、第三、及び第四アミノ酸配列を
含んで成る; q)前記少なくとも第一表面を注目の抗体に暴露し、該
注目の抗体が前記第一、第二、第三又は第四アミノ酸配
列の少なくとも1つにより強く結合する; r)前記少なくとも第一表面を受容体に暴露し、該受容
体は前記注目の抗体を認識しそしてその複数の場所にお
いて結合し、該受容体はフルオレッセインを含んで成
る; s)前記少なくとも第一表面に光を暴露し、該第一表面
は少なくとも前記より強く結合したアミノ酸配列が位置
する領域において蛍光を発する;並びに t)前記少なくとも第一表面を横切る場所に関数として
蛍光の強度を検出及び記録する;段階を含んで成る方
法。 - 【請求項2】 受容体との結合について少なくとも1つ
のペプチド配列を同定する方法であって、 a)各々が光除去可能な保護基を有する複数のポリペプ
チドを有する基体上で、第一の選択されたポリペプチド
を照射することによって前記保護基を除去する; b)前記ポリペプチドを第一アミノ酸と接触せしめるこ
とにより第一配列を生成せしめ、前記基体上の第二ポリ
ペプチドは第二配列を含んで成る;及び c)前記第一配列又は第二配列のいずれが前記受容体と
結合するかを同定する;段階を含んで成る方法。 - 【請求項3】 表面を有する基体を含んで成るポリマー
をスクリーニングするための装置であって、該表面は少
なくとも2個のあらかじめ定められた領域を含んで成
り、該あらかじめ定められた領域はその上に異るモノマ
ー配列を含み、該あらかじめ定められた領域の各々が約
0.1cm2 未満の面積を占めることを特徴とする装置。 - 【請求項4】 前記面積が約0.01cm2 未満である、
請求項3に記載の装置。 - 【請求項5】 前記面積が10000μm2 未満であ
る、請求項3に記載の装置。 - 【請求項6】 前記面積が100μm2 未満である、請
求項3に記載の装置。 - 【請求項7】 前記モノマー配列が前記あらかじめ定め
られた領域内で実質的に純粋である、請求項3,4,5
又は6に記載の装置。 - 【請求項8】 その表面上のあらかじめ定められた領域
に103 又はそれより多くの異るリガンドを含んで成
る、生物学的活性についてスクリーニングするための基
体。 - 【請求項9】 前記基体があらかじめ定められた領域内
に104 又はそれより多くの異るリガンドを含んで成
る、請求項8に記載の基体。 - 【請求項10】 前記基体があらかじめ定められた領域
内に105 又はそれより多くの異るリガンドを含んで成
る、請求項8に記載の基体。 - 【請求項11】 前記基体があらかじめ定められた領域
内に106 又はそれより多くのリガンドを含んで成る、
請求項8に記載の基体。 - 【請求項12】 前記リガンドがペプチドである、請求
項8,9,10又は11に記載の基体。 - 【請求項13】 前記リガンドが前記あらかじめ定めら
れた領域内で実質的に純粋である、請求項11に記載の
基体。 - 【請求項14】 生物学的活性についてスクリーニング
するための装置であって、 a)複数のポリマー配列を含んで成る基体(該ポリマー
配列は該基体上の既知の場所において該基体の表面に結
合されており、該配列の各々は約0.1cm2 未満の面積
を占めている); b)蛍光標識により標識されており前記配列の少なくと
も1つと結合する受容体に前記基体と暴露する手段;並
びに c)前記基体上の前記蛍光標識の場所を検出するための
手段;を含んで成る装置。 - 【請求項15】 基体上の蛍光標識された領域を検出す
るための装置であって、 a)前記基体の表面に光をむけるための光源; b)前記光源に応答して前記表面から発生した蛍光を検
出する手段; c)前記基体を第一位置から第二位置に移行するための
手段;並びに d)前記基体上の場所の関数として蛍光強度を格納する
ための、前記移行手段及び前記検出手段に連絡された手
段;を含んで成る装置。 - 【請求項16】 その表面上の所定の領域に100以上
の異るオリゴヌクレオチドを有するハイブリダイゼーシ
ョン用基体。 - 【請求項17】 所定の領域に103 以上の異るオリゴ
ヌクレオチドを有する請求項16に記載の基体。 - 【請求項18】 所望の領域に104 以上のオリゴヌク
レオチドを有する請求項16に記載の基体。 - 【請求項19】 所望の領域に105 以上の異るオリゴ
ヌクレオチドを有する請求項17に記載の基体。 - 【請求項20】 所定の領域に106 以上の異るオリゴ
ヌクレオチドを有する請求項16に記載の基体。 - 【請求項21】 所望の領域に107 以上の異るオリゴ
ヌクレオチドを有する請求項16に記載の基体。 - 【請求項22】 前記オリゴヌクレオチドの各々が約
0.1cm2 未満の面積を占める、請求項17〜21のい
ずれか1項に記載の基体。 - 【請求項23】 前記所定の領域が該所定の領域内で実
質的に純粋である、請求項16〜21のいずれか1項に
記載の基体。 - 【請求項24】 前記オリゴヌクレオチド配列が0.1
cm2 未満の面積に含まれる、請求項17〜22のいずれ
か1項に記載の基体。
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US36290189A | 1989-06-07 | 1989-06-07 | |
US362901 | 1989-06-07 | ||
US492462 | 1990-03-07 | ||
US07/492,462 US5143854A (en) | 1989-06-07 | 1990-03-07 | Large scale photolithographic solid phase synthesis of polypeptides and receptor binding screening thereof |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP50896690A Division JP3759161B2 (ja) | 1989-06-07 | 1990-06-07 | 非常に大規模な固定化ペプチド合成 |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH1121293A true JPH1121293A (ja) | 1999-01-26 |
Family
ID=27001838
Family Applications (5)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP50896690A Expired - Lifetime JP3759161B2 (ja) | 1989-06-07 | 1990-06-07 | 非常に大規模な固定化ペプチド合成 |
JP8324451A Withdrawn JPH1121293A (ja) | 1989-06-07 | 1996-12-04 | 非常に大規模な固定化ペプチドの合成 |
JP11049217A Withdrawn JPH11315095A (ja) | 1989-06-07 | 1999-02-25 | 非常に大規模な固定化ペプチド合成 |
JP2003112204A Withdrawn JP2004002386A (ja) | 1989-06-07 | 2003-04-16 | 非常に大規模な固定化ペプチド合成 |
JP2005018992A Withdrawn JP2005112867A (ja) | 1989-06-07 | 2005-01-26 | 非常に大規模な固定化ペプチド合成 |
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JP50896690A Expired - Lifetime JP3759161B2 (ja) | 1989-06-07 | 1990-06-07 | 非常に大規模な固定化ペプチド合成 |
Family Applications After (3)
Application Number | Title | Priority Date | Filing Date |
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JP11049217A Withdrawn JPH11315095A (ja) | 1989-06-07 | 1999-02-25 | 非常に大規模な固定化ペプチド合成 |
JP2003112204A Withdrawn JP2004002386A (ja) | 1989-06-07 | 2003-04-16 | 非常に大規模な固定化ペプチド合成 |
JP2005018992A Withdrawn JP2005112867A (ja) | 1989-06-07 | 2005-01-26 | 非常に大規模な固定化ペプチド合成 |
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US (19) | US5143854A (ja) |
EP (4) | EP0619321B1 (ja) |
JP (5) | JP3759161B2 (ja) |
KR (2) | KR970001577B1 (ja) |
AT (2) | ATE175421T1 (ja) |
AU (2) | AU651795B2 (ja) |
BR (1) | BR9007425A (ja) |
CA (4) | CA2278883C (ja) |
DE (3) | DE69012119T2 (ja) |
DK (2) | DK0619321T3 (ja) |
ES (2) | ES2129101T3 (ja) |
FI (1) | FI109130B (ja) |
GB (1) | GB2248840B (ja) |
HK (2) | HK64195A (ja) |
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IL (1) | IL94551A (ja) |
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JP2002536977A (ja) * | 1999-02-19 | 2002-11-05 | フェビット フェラリウス バイオテクノロジー ゲゼルシャフト ミット ベシュレンクテル ハフツング | ポリマーの製法 |
US8697349B2 (en) | 2007-11-01 | 2014-04-15 | Kabushiki Kaisha Toyota Chuo Kenkyusho | Method of producing solid-phase body having immobilized microobject and the use thereof |
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US5866363A (en) | 1985-08-28 | 1999-02-02 | Pieczenik; George | Method and means for sorting and identifying biological information |
US6270961B1 (en) * | 1987-04-01 | 2001-08-07 | Hyseq, Inc. | Methods and apparatus for DNA sequencing and DNA identification |
GB8810400D0 (en) | 1988-05-03 | 1988-06-08 | Southern E | Analysing polynucleotide sequences |
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JP2002536977A (ja) * | 1999-02-19 | 2002-11-05 | フェビット フェラリウス バイオテクノロジー ゲゼルシャフト ミット ベシュレンクテル ハフツング | ポリマーの製法 |
US8697349B2 (en) | 2007-11-01 | 2014-04-15 | Kabushiki Kaisha Toyota Chuo Kenkyusho | Method of producing solid-phase body having immobilized microobject and the use thereof |
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