JP2020511996A - 改変イガイタンパク質類、それらの使用及び関連化合物 - Google Patents
改変イガイタンパク質類、それらの使用及び関連化合物 Download PDFInfo
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- dihydroxyphenylalanine
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43509—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from crustaceans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L24/00—Surgical adhesives or cements; Adhesives for colostomy devices
- A61L24/001—Use of materials characterised by their function or physical properties
- A61L24/0042—Materials resorbable by the body
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L24/00—Surgical adhesives or cements; Adhesives for colostomy devices
- A61L24/04—Surgical adhesives or cements; Adhesives for colostomy devices containing macromolecular materials
- A61L24/10—Polypeptides; Proteins
- A61L24/108—Specific proteins or polypeptides not covered by groups A61L24/102 - A61L24/106
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/93—Ligases (6)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y601/00—Ligases forming carbon-oxygen bonds (6.1)
- C12Y601/01—Ligases forming aminoacyl-tRNA and related compounds (6.1.1)
- C12Y601/01014—Glycine-tRNA ligase (6.1.1.14)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/55—Design of synthesis routes, e.g. reducing the use of auxiliary or protecting groups
Abstract
Description
以下において引用される文献または関連する文献としては、以下の非特許文献がある。
保護された3,4−ジヒドロキシフェニルアラニン誘導体を生成するために、多くの一般に知られている保護基を使用でき、Dopaの接着特性の時空間的な活性化を可能にする。
ONB−Dopaを、この例示全体を通して、保護された(光ケージド)3,4−ジヒドロキシフェニルアラニン誘導体残基として使用した。
Claims (17)
- 改変イガイ接着タンパク質であって、カテコール部分の少なくとも1つの水酸基残基への保護基を含む、少なくとも1つの光ケージド3,4−ジヒドロキシフェニルアラニン誘導体残基を備え、前記光ケージド3,4−ジヒドロキシフェニルアラニン誘導体残基は、天然のアミノ酸を置換し、前記保護基を、UV光での照射により、前記3,4−ジヒドロキシフェニルアラニン誘導体残基から切断できる、改変イガイ接着タンパク質。
- 請求項1に記載の改変イガイ接着タンパク質において、改変fp−5タンパク質であることを特徴とする、改変イガイ接着タンパク質。
- 請求項1又は2に記載の改変イガイ接着タンパク質において、前記光ケージド3,4−ジヒドロキシフェニルアラニン誘導体残基が、チロシン残基を置換することを特徴とする、改変イガイ接着タンパク質。
- 請求項1〜3のいずれか一項に記載の改変イガイ接着タンパク質において、前記光ケージド3,4−ジヒドロキシフェニルアラニン誘導体残基が、オルト−ニトロベンジル−3,4−ジヒドロキシフェニルアラニン残基であることを特徴とする、改変イガイ接着タンパク質。
- 請求項1〜3のいずれか一項に記載の改変イガイ接着タンパク質において、配列番号14、配列番号15、配列番号16、配列番号17、配列番号18又は配列番号19と少なくとも95%同一であるアミノ酸配列を含む、改変イガイ接着タンパク質。
- 請求項1〜5のいずれか一項に記載の改変イガイ接着タンパク質において、配列番号1、配列番号2、配列番号3、配列番号11、配列番号12又は配列番号13と少なくとも95%同一であるアミノ酸配列を含む、改変イガイ接着タンパク質。
- 請求項5又は6に記載の改変イガイ接着タンパク質において、請求項5又は6で定義された前記アミノ酸配列のN末端に融合している、配列番号4と少なくとも95%同一であるアミノ酸配列を含む、改変イガイ接着タンパク質。
- インビトロでの生分解性接着剤としての、請求項1〜7のいずれか一項に記載の改変イガイ接着タンパク質の使用。
- 表面を、前記改変イガイタンパク質に共有結合している機能的本体でインビトロ被覆するための、請求項1〜7のいずれか一項に記載の改変イガイ接着タンパク質の使用。
- 請求項9に記載の使用において、前記機能的本体が、抗菌特性を示すことを特徴とする、使用。
- 外科手術における使用又は治療における使用のための、特に、生分解性接着剤としての、請求項1〜7のいずれか一項に記載の改変イガイ接着タンパク質。
- 骨折の処置における使用のための又は創傷治癒を促進するための、請求項1〜7のいずれか一項に記載の改変イガイ接着タンパク質。
- 配列番号5、配列番号6又は配列番号7と少なくとも99%同一である配列を有する、請求項7に記載の改変イガイ接着タンパク質をコードする核酸。
- 配列番号8、配列番号9又は配列番号10と少なくとも98%同一であるアミノ酸配列を含む、アミノアシル−tRNAシンターゼ。
- 合成されるペプチドにオルト−ニトロベンジル−3,4−ジヒドロキシフェニルアラニンを組み込むための、請求項14に記載のアミノアシル−tRNAシンターゼの使用。
- ペプチドの合成中でのカテコール部分の少なくとも1つの水酸基残基へのUV光の照射により切断できる保護基を含む、光ケージド3,4−ジヒドロキシフェニルアラニン誘導体の使用。
- 請求項16に記載の使用において、前記光ケージド3,4−ジヒドロキシフェニルアラニン誘導体残基が、オルト−ニトロベンジル−3,4−ジヒドロキシフェニルアラニンであることを特徴とする、使用。
Applications Claiming Priority (3)
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PCT/EP2018/057641 WO2018178013A1 (en) | 2017-03-28 | 2018-03-26 | Modified mussel proteins, uses thereof and related compounds |
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JP (1) | JP7253804B2 (ja) |
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JP2008504016A (ja) * | 2004-03-26 | 2008-02-14 | ポスコ | イガイ接着蛋白質 |
JP2014161229A (ja) * | 2013-02-21 | 2014-09-08 | National Institute Of Agrobiological Sciences | タンパク質の発現を制御する方法 |
WO2016210350A1 (en) * | 2015-06-25 | 2016-12-29 | Amyris, Inc. | Maltose dependent degrons, maltose-responsive promoters, stabilization constructs, and their use in production of non-catabolic compounds |
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US5202236A (en) * | 1984-09-13 | 1993-04-13 | Enzon Labs Inc. | Method of producing bioadhesive protein |
US7083970B2 (en) | 2001-04-19 | 2006-08-01 | The Scripps Research Institute | Methods and compositions for the production of orthogonal tRNA-aminoacyl tRNA synthetase pairs |
JP2008513040A (ja) | 2004-09-21 | 2008-05-01 | ザ スクリップス リサーチ インスティテュート | 光調節型アミノ酸の遺伝コード付加 |
CA2608192A1 (en) * | 2005-06-03 | 2006-12-14 | Ambrx, Inc. | Incorporation of non-naturally encoded amino acids into proteins |
WO2015126480A2 (en) * | 2013-11-13 | 2015-08-27 | Massachusetts Institute Of Technology | Self-assembling underwater adhesives |
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JP2008504016A (ja) * | 2004-03-26 | 2008-02-14 | ポスコ | イガイ接着蛋白質 |
JP2014161229A (ja) * | 2013-02-21 | 2014-09-08 | National Institute Of Agrobiological Sciences | タンパク質の発現を制御する方法 |
WO2016210350A1 (en) * | 2015-06-25 | 2016-12-29 | Amyris, Inc. | Maltose dependent degrons, maltose-responsive promoters, stabilization constructs, and their use in production of non-catabolic compounds |
Non-Patent Citations (1)
Title |
---|
西田仁 他: "XV.グリーンマテリアルの新展開 (9)接着性タンパク質模倣高分子材,カテコール系高分子", 日本接着学会誌, vol. 49(10), JPN7022000346, 2013, pages 389 - 395, ISSN: 0004792868 * |
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US20210087237A1 (en) | 2021-03-25 |
WO2018178013A1 (en) | 2018-10-04 |
KR20190133218A (ko) | 2019-12-02 |
CA3058273A1 (en) | 2018-10-04 |
US11345910B2 (en) | 2022-05-31 |
EP3601323A1 (en) | 2020-02-05 |
CN110461867A (zh) | 2019-11-15 |
JP7253804B2 (ja) | 2023-04-07 |
EP3381932A1 (en) | 2018-10-03 |
EP3601323B1 (en) | 2022-05-04 |
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