JP2013181021A - Artificial peptide with rare metal binding capacity, and use of the same - Google Patents
Artificial peptide with rare metal binding capacity, and use of the same Download PDFInfo
- Publication number
- JP2013181021A JP2013181021A JP2012047585A JP2012047585A JP2013181021A JP 2013181021 A JP2013181021 A JP 2013181021A JP 2012047585 A JP2012047585 A JP 2012047585A JP 2012047585 A JP2012047585 A JP 2012047585A JP 2013181021 A JP2013181021 A JP 2013181021A
- Authority
- JP
- Japan
- Prior art keywords
- peptide
- amino acid
- metal
- rare metal
- palladium
- 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.)
- Granted
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- 239000007788 liquid Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- VZCYOOQTPOCHFL-UPHRSURJSA-N maleic acid Chemical compound OC(=O)\C=C/C(O)=O VZCYOOQTPOCHFL-UPHRSURJSA-N 0.000 description 1
- 239000011976 maleic acid Substances 0.000 description 1
- 239000001630 malic acid Substances 0.000 description 1
- 235000011090 malic acid Nutrition 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- 125000004108 n-butyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 125000004123 n-propyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 125000001624 naphthyl group Chemical group 0.000 description 1
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 description 1
- ZQPPMHVWECSIRJ-KTKRTIGZSA-N oleic acid Chemical compound CCCCCCCC\C=C/CCCCCCCC(O)=O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 1
- 235000021313 oleic acid Nutrition 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 229910052762 osmium Inorganic materials 0.000 description 1
- SYQBFIAQOQZEGI-UHFFFAOYSA-N osmium atom Chemical compound [Os] SYQBFIAQOQZEGI-UHFFFAOYSA-N 0.000 description 1
- 235000006408 oxalic acid Nutrition 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000010970 precious metal Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 239000010948 rhodium Substances 0.000 description 1
- 229910052703 rhodium Inorganic materials 0.000 description 1
- MHOVAHRLVXNVSD-UHFFFAOYSA-N rhodium atom Chemical compound [Rh] MHOVAHRLVXNVSD-UHFFFAOYSA-N 0.000 description 1
- 229910052707 ruthenium Inorganic materials 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 239000011975 tartaric acid Substances 0.000 description 1
- 235000002906 tartaric acid Nutrition 0.000 description 1
- YBRBMKDOPFTVDT-UHFFFAOYSA-N tert-butylamine Chemical compound CC(C)(C)N YBRBMKDOPFTVDT-UHFFFAOYSA-N 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
Classifications
-
- 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
- Y02P10/00—Technologies related to metal processing
- Y02P10/20—Recycling
Landscapes
- Peptides Or Proteins (AREA)
- Manufacture And Refinement Of Metals (AREA)
- Investigating Or Analyzing Non-Biological Materials By The Use Of Chemical Means (AREA)
- Water Treatment By Sorption (AREA)
- Solid-Sorbent Or Filter-Aiding Compositions (AREA)
Abstract
Description
本発明は、レアメタル結合能を有する人工ペプチドおよびその利用に関するものであり、詳細には、レアメタル結合能を有する人工ペプチドを含有する金属吸着剤、それを用いるレアメタル回収方法、レアメタル検出方法に関するものである。 The present invention relates to an artificial peptide having a rare metal binding ability and use thereof, and more particularly to a metal adsorbent containing an artificial peptide having a rare metal binding ability, a rare metal recovery method using the same, and a rare metal detection method. is there.
先端科学技術の発展に深く関わり、高性能化の材料となっているのがレアメタルとよばれる非鉄金属類であり、材料・触媒化学の分野において広く注目を浴びている。近年の技術革新や新興国の発展に伴い、貴金属をはじめとするレアメタルの使用量が急増しており、資源確保観点からも金属の回収法の効率化が急務の課題となっている。 Deeply involved in the development of advanced science and technology, non-ferrous metals called rare metals are becoming high-performance materials, and are attracting widespread attention in the field of materials and catalytic chemistry. With recent technological innovation and the development of emerging countries, the use of rare metals including precious metals has increased rapidly, and from the viewpoint of securing resources, the efficiency of metal recovery methods has become an urgent issue.
従来のレアメタル回収技術は、高温や強酸性など極端な条件で行われるため、環境負荷が大きく、エネルギー消費も大きい。また、特定のレアメタルのみを選択的に回収することは困難である。そこで、環境負荷の少ないレアメタル回収技術が求められており、種々の技術が提案されている（例えば、特許文献１参照）。 Conventional rare metal recovery technology is performed under extreme conditions such as high temperature and strong acidity, and therefore has a large environmental load and energy consumption. In addition, it is difficult to selectively recover only specific rare metals. Thus, a rare metal recovery technique with a low environmental load is required, and various techniques have been proposed (for example, see Patent Document 1).
本発明は、レアメタル結合能を有する人工ペプチドを提供し、環境負荷の少ないレアメタル回収方法を提供することを課題とする。 An object of the present invention is to provide an artificial peptide having a rare metal binding ability, and to provide a method for recovering a rare metal with less environmental load.
本発明は、上記課題を解決するために、以下の各発明を包含する。
［１］以下のアミノ酸配列（１）を有し、かつアミノ酸残基数が１００以下であるペプチド。
（１）ＳＤＰＬＶＸ１ＲＡＳＬＩＧＬＬＸ２ＬＬＬＷＸ３Ｘ４Ｘ５ＲＸ６（配列番号１）
（Ｘ１は親水性アミノ酸、Ｘ２はＨまたはＡ、Ｘ３はＲまたはＫ、Ｘ４はＭまたは脂肪族アミノ酸、Ｘ５はＤまたはＥ、Ｘ６は任意のアミノ酸を表す。）
［２］Ｘ１がＮまたはＲ、Ｘ４がＭまたはＬ、Ｘ６がＫまたはＬである前記［１］に記載のペプチド。
［３］アミノ酸配列（１）が、以下のアミノ酸配列（２）または（３）である前記［２］に記載のペプチド。
（２）ＳＤＰＬＶＮＲＡＳＬＩＧＬＬＨＬＬＬＷＲＭＤＲＬ（配列番号２）
（３）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＭＤＲＫ（配列番号３）
［４］アミノ酸配列（１）が、以下のアミノ酸配列（４）または（５）である前記［２］に記載のペプチド。
（４）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＬＥＲＫ（配列番号４）
（５）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＡＬＬＬＷＫＭＤＲＫ（配列番号５）
［５］前記［１］〜［４］のいずれかに記載のペプチドを含有する金属吸着剤。
［６］金属がレアメタルである前記［５］に記載の金属吸着剤。
［７］レアメタルがパラジウムおよび／または白金である前記［６］に記載の金属吸着剤。
［８］前記［５］〜［７］のいずれかに記載の金属吸着材とレアメタルを含む金属成分を含有する水溶液とを接触させる工程とを含むことを特徴とするレアメタル回収方法。
［９］レアメタルがパラジウムおよび／または白金である前記［８］に記載のレアメタル回収方法。
［１０］前記［１］〜［４］のいずれかに記載のペプチドとレアメタルを含む金属成分を含有する水溶液とを接触させる工程、および、当該ペプチドの構造変化を検出する工程を含むことを特徴とするレアメタル検出方法。
［１１］レアメタルがパラジウムおよび／または白金である前記［１０］に記載のレアメタル検出方法。
The present invention includes the following inventions in order to solve the above problems.
[1] A peptide having the following amino acid sequence (1) and having 100 or fewer amino acid residues.
(1) SDPLVX 1 RASLIGLLX 2 LLLWX 3 X 4 X 5 RX 6 (SEQ ID NO: 1)
(X 1 represents a hydrophilic amino acid, X 2 represents H or A, X 3 represents R or K, X 4 represents M or an aliphatic amino acid, X 5 represents D or E, and X 6 represents any amino acid.)
[2] The peptide according to [1], wherein X 1 is N or R, X 4 is M or L, and X 6 is K or L.
[3] The peptide according to [2], wherein the amino acid sequence (1) is the following amino acid sequence (2) or (3).
(2) SDPLVNRASLIGLLLHLLWRMDRL (SEQ ID NO: 2)
(3) SDPLVRRASLIGLLLHLLWKMDRK (SEQ ID NO: 3)
[4] The peptide according to [2], wherein the amino acid sequence (1) is the following amino acid sequence (4) or (5).
(4) SDPLVRRASLIGLLLHLLWKLERK (SEQ ID NO: 4)
(5) SDPLVRRASLIGLALLLLWKMDRK (SEQ ID NO: 5)
[5] A metal adsorbent containing the peptide according to any one of [1] to [4].
[6] The metal adsorbent according to [5], wherein the metal is a rare metal.
[7] The metal adsorbent according to [6], wherein the rare metal is palladium and / or platinum.
[8] A method for recovering a rare metal, comprising a step of bringing the metal adsorbent according to any one of [5] to [7] into contact with an aqueous solution containing a metal component containing a rare metal.
[9] The rare metal recovery method according to [8], wherein the rare metal is palladium and / or platinum.
[10] The method includes contacting the peptide according to any one of [1] to [4] above with an aqueous solution containing a metal component containing a rare metal, and detecting a structural change of the peptide. Rare metal detection method.
[11] The rare metal detection method according to [10], wherein the rare metal is palladium and / or platinum.
本発明によれば、レアメタル結合能を有する人工ペプチドを提供することができる。当該人工ペプチドは、金属吸着材として好適に使用することができる。当該金属吸着材を用いることにより、レアメタルを効率よく回収することができる。 According to the present invention, an artificial peptide having a rare metal binding ability can be provided. The artificial peptide can be suitably used as a metal adsorbent. By using the metal adsorbent, the rare metal can be efficiently recovered.
Ｍ２タンパク質はＡ型インフルエンザウイルスのエンベロープ内に存在する膜タンパク質である。Ｍ２タンパク質は、９７残基のアミノ酸（配列番号６）からなる１回膜貫通タンパク質であり、天然状態ではヘリックス構造をとっておりテトラマーを構成している。さらに、その４本膜貫通ヘリックスはｐＨ依存性のプロトンチャネルを形成しており、その中に含むＨｉｓ３７はｐＨセンサーであり、Ｔｒｐ４１はゲートの役割を担っている（Jasen R. Schnell et al., Nature 451 591-595 2008. 、Stouffer AL et al., Nature 451 596-599 2008.）。また、Ｍ２タンパク質は銅イオンと選択的に結合する能力を保有していることが知られている（Chris S. Gandhi et al., J Biol Chem 274(9) 5474-82 1999）。
そこで、本発明者らは、Ｍ２タンパク質の膜貫通ドメインを含むＳｅｒ２３からＬｅｕ４６までのアミノ酸配列からなるペプチドは疎水性が高く水に不溶であったためアミノ酸配列を改変することで水溶性を獲得させ、さらに新たな金属結合能を付与するべくペプチド分子を設計し、種々の性質について検討を行った。その結果、レアメタル結合能を有する水溶性アナログを見出し、本発明を完成させるに至った。
M2 protein is a membrane protein present in the envelope of influenza A virus. The M2 protein is a single-transmembrane protein consisting of 97 amino acids (SEQ ID NO: 6). In the natural state, the M2 protein has a helical structure and constitutes a tetramer. Furthermore, the four transmembrane helix forms a pH-dependent proton channel, His37 contained therein is a pH sensor, and Trp41 plays a role of a gate (Jasen R. Schnell et al.,). Nature 451 591-595 2008., Stouffer AL et al., Nature 451 596-599 2008.). It is also known that M2 protein possesses the ability to selectively bind to copper ions (Chris S. Gandhi et al., J Biol Chem 274 (9) 5474-82 1999).
Therefore, the present inventors acquired a water-solubility by altering the amino acid sequence because the peptide consisting of the amino acid sequence from Ser23 to Leu46 containing the transmembrane domain of M2 protein was highly hydrophobic and insoluble in water. Furthermore, peptide molecules were designed to give new metal binding ability, and various properties were examined. As a result, a water-soluble analog having a rare metal binding ability was found and the present invention was completed.
〔ペプチド〕
本発明は、以下のアミノ酸配列（１）を有し、かつアミノ酸残基数が１００以下であるペプチドを提供する。
（１）ＳＤＰＬＶＸ１ＲＡＳＬＩＧＬＬＸ２ＬＬＬＷＸ３Ｘ４Ｘ５ＲＸ６（配列番号１）
（Ｘ１は親水性アミノ酸、Ｘ２はＨまたはＡ、Ｘ３はＲまたはＫ、Ｘ４はＭまたは脂肪族アミノ酸、Ｘ５はＤまたはＥ、Ｘ６は任意のアミノ酸を表す。）
本発明のペプチドは、水溶性かつレアメタル結合能を有しているペプチドであればよい。本発明のペプチドは、上記アミノ酸配列（１）を含むものであればよく、それ以外の部分のアミノ酸配列は、水溶性およびレアメタル結合能の少なくとも一方を損なわない限り特に限定されない。なお、本明細書において、「ペプチド」は２個以上のアミノ酸がペプチド結合によって結合したものを意味し、結合するアミノ酸の数は問わない。すなわち、本発明における「ペプチド」にはポリペプチドが含まれる。
〔peptide〕
The present invention provides a peptide having the following amino acid sequence (1) and having 100 or fewer amino acid residues.
(1) SDPLVX 1 RASLIGLLX 2 LLLWX 3 X 4 X 5 RX 6 (SEQ ID NO: 1)
(X 1 represents a hydrophilic amino acid, X 2 represents H or A, X 3 represents R or K, X 4 represents M or an aliphatic amino acid, X 5 represents D or E, and X 6 represents any amino acid.)
The peptide of the present invention may be any peptide that is water-soluble and has a rare metal binding ability. The peptide of this invention should just contain the said amino acid sequence (1), and the amino acid sequence of a part other than that is not specifically limited unless at least one of water solubility and a rare metal binding ability is impaired. In the present specification, “peptide” means a peptide in which two or more amino acids are bound by peptide bonds, and the number of bound amino acids is not limited. That is, the “peptide” in the present invention includes a polypeptide.
Ｘ１は親水性アミノ酸であればよい。Ｘ１の親水性アミノ酸としては、例えばアスパラギン、アルギニン、アスパラギン酸、グルタミン酸、グルタミン、ヒスチジン、リジン、セリン、トレオニン等が挙げられる。好ましくは、アスパラギン、アルギニンまたはグルタミン酸である。
Ｘ４はメチオニンまたは脂肪族アミノ酸であればよい。Ｘ４の脂肪族アミノ酸としては、例えばロイシン、イソロイシン、アラニン、バリン等が挙げられる。好ましくはロイシンである。
Ｘ６のアミノ酸は特に限定されず、いずれのアミノ酸でもよい。好ましくは、ロイシン、リジン、グリシンであり、より好ましくは、ロイシンまたはリジンである。
X 1 may be a hydrophilic amino acid. The hydrophilic amino acids X 1, for example asparagine, arginine, aspartic acid, glutamic acid, glutamine, histidine, lysine, serine, threonine, and the like. Preferred is asparagine, arginine or glutamic acid.
X 4 may be methionine or an aliphatic amino acid. Examples of the aliphatic amino acid X 4 include leucine, isoleucine, alanine, valine and the like. Preferred is leucine.
Amino acid X 6 is not particularly limited, and may be any amino acid. Preferred are leucine, lysine and glycine, and more preferred is leucine or lysine.
上記アミノ酸配列（１）は、以下のアミノ酸配列（２）または（３）であることが好ましい。
（２）ＳＤＰＬＶＮＲＡＳＬＩＧＬＬＨＬＬＬＷＲＭＤＲＬ（配列番号２）
（３）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＭＤＲＫ（配列番号３）
アミノ酸配列（２）または（３）からなるペプチドは水溶性であり、パラジウムおよび銅と選択的に結合することが確認されている。
The amino acid sequence (1) is preferably the following amino acid sequence (2) or (3).
(2) SDPLVNRASLIGLLLHLLWRMDRL (SEQ ID NO: 2)
(3) SDPLVRRASLIGLLLHLLWKMDRK (SEQ ID NO: 3)
The peptide consisting of the amino acid sequence (2) or (3) is water-soluble and has been confirmed to bind selectively to palladium and copper.
また、上記アミノ酸配列（１）は、以下のアミノ酸配列（４）または（５）であることが好ましい。
（４）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＬＥＲＫ（配列番号４）
（５）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＡＬＬＬＷＫＭＤＲＫ（配列番号５）
アミノ酸配列（４）または（５）からなるペプチドは水溶性であり、パラジウムと選択的に結合することが確認されている。
The amino acid sequence (1) is preferably the following amino acid sequence (4) or (5).
(4) SDPLVRRASLIGLLLHLLWKLERK (SEQ ID NO: 4)
(5) SDPLVRRASLIGLALLLLWKMDRK (SEQ ID NO: 5)
The peptide consisting of the amino acid sequence (4) or (5) is water-soluble and has been confirmed to selectively bind to palladium.
本発明のペプチドのアミノ酸残基数は、２４残基以上１００残基以下であれば特に限定されない。取り扱いの簡便さ、製造効率等の観点から、アミノ酸残基数の上限は約８０残基が好ましく、より好ましくは約５０残基、さらに好ましくは約４０残基、特に好ましくは約３０残基である。 The number of amino acid residues of the peptide of the present invention is not particularly limited as long as it is 24 residues or more and 100 residues or less. From the viewpoint of easy handling and production efficiency, the upper limit of the number of amino acid residues is preferably about 80 residues, more preferably about 50 residues, still more preferably about 40 residues, and particularly preferably about 30 residues. is there.
本発明のペプチドの具体例としては、例えば、配列番号６のアミノ酸配列からなるＭ２タンパク質のＳｅｒ２３からＬｅｕ４６を、上記アミノ酸配列（１）で置換したペプチドを含むペプチドを好適に用いることができる。また、上記アミノ酸配列（１）を２〜４回繰り返した配列を含むペプチドを好適に用いることができる。上記アミノ酸配列（１）を２〜４回繰り返した配列としては、具体的には、例えば、上記アミノ酸配列（２）〜（５）のいずれか１種を２〜４回繰り返した配列、上記アミノ酸配列（２）〜（５）の２〜４種を適宜組み合わせて結合した配列などが挙げられる。好ましくは上記アミノ酸配列（２）〜（５）のいずれか１種からなるペプチドであり、より好ましくは上記アミノ酸配列（４）または（５）からなるペプチドである。 As a specific example of the peptide of the present invention, for example, a peptide containing a peptide obtained by substituting Ser23 to Leu46 of M2 protein consisting of the amino acid sequence of SEQ ID NO: 6 with the amino acid sequence (1) can be preferably used. Moreover, the peptide containing the sequence which repeated the said amino acid sequence (1) 2-4 times can be used conveniently. Specific examples of the sequence in which the amino acid sequence (1) is repeated 2 to 4 times include, specifically, a sequence in which any one of the amino acid sequences (2) to (5) is repeated 2 to 4 times, the amino acid Examples include sequences in which 2 to 4 types of sequences (2) to (5) are combined in an appropriate combination. A peptide consisting of any one of the amino acid sequences (2) to (5) is preferred, and a peptide consisting of the amino acid sequence (4) or (5) is more preferred.
本発明のペプチドは、公知の一般的なペプチド合成のプロトコールに従って、固相合成法（Ｆｍｏｃ法、Ｂｏｃ法）または液相合成法により製造することができる。また、本発明のペプチドをコードするＤＮＡを含有する発現ベクターを導入した形質転換体を用いる方法や、ｉｎ ｖｉｔｒｏ転写・翻訳系を用いる方法により製造することができる。 The peptide of the present invention can be produced by a solid phase synthesis method (Fmoc method, Boc method) or a liquid phase synthesis method according to a known general peptide synthesis protocol. Further, it can be produced by a method using a transformant into which an expression vector containing a DNA encoding the peptide of the present invention has been introduced, or a method using an in vitro transcription / translation system.
本発明のペプチドは、Ｃ末端がカルボキシル基（−ＣＯＯＨ）、カルボキシレート(−ＣＯＯ−)、アミド（−ＣＯＮＨ２）またはエステル（−ＣＯＯＲ）の何れであってもよい。エステルにおけるＲとしては、例えば、メチル、エチル、ｎ−プロピル、イソプロピルもしくはｎ−ブチルなどのＣ１−６アルキル基、例えば、シクロペンチル、シクロヘキシルなどのＣ３−８シクロアルキル基、例えば、フェニル、α−ナフチルなどのＣ６−１２アリール基、例えば、ベンジル、フェネチルなどのフェニル−Ｃ１−２アルキル基もしくはα−ナフチルメチルなどのα−ナフチル−Ｃ１−２アルキル基などのＣ７−１４アラルキル基のほか、経口用エステルとして汎用されるピバロイルオキシメチル基などが挙げられる。本発明のペプチドがＣ末端以外にカルボキシル基またはカルボキシレートを有している場合、それらの基がアミド化またはエステル化されているものも本発明のペプチドに含まれる。 In the peptide of the present invention, the C-terminus may be any of a carboxyl group (—COOH), a carboxylate (—COO − ), an amide (—CONH 2 ), or an ester (—COOR). As R in the ester, for example, a C 1-6 alkyl group such as methyl, ethyl, n-propyl, isopropyl or n-butyl, for example, a C 3-8 cycloalkyl group such as cyclopentyl, cyclohexyl, for example, phenyl, α - C 6-12 aryl group such as naphthyl, for example, benzyl, C 7 - 14 aralkyl such as α- naphthyl -C 1-2 alkyl group such as a phenyl -C 1-2 alkyl or α- naphthylmethyl such phenethyl In addition to the group, a pivaloyloxymethyl group, which is widely used as an oral ester, can be mentioned. When the peptide of the present invention has a carboxyl group or a carboxylate other than the C-terminus, those in which these groups are amidated or esterified are also included in the peptide of the present invention.
本発明のペプチドを構成するアミノ酸は、側鎖が任意の置換基で修飾されたものでもよい。置換基は特に限定されないが、例えば、フッ素原子、塩素原子、シアノ基、水酸基、ニトロ基、アルキル基、シクロアルキル基、アルコキシ基、アミノ基などが挙げられる。 さらに、本発明のペプチドには、Ｎ末端のメチオニン残基のアミノ基が保護基（例えば、ホルミル基、アセチルなどのＣ２−６アルカノイル基などのＣ１−６アシル基など）で保護されているもの、Ｎ末端側が生体内で切断され生成したグルタミル基がピログルタミン酸化したもの、分子内のアミノ酸の側鎖上の置換基（例えば、−ＯＨ、−ＳＨ、アミノ基、イミダゾール基、インドール基、グアニジノ基など）が適当な保護基（例えば、ホルミル基、アセチルなどのＣ２−６アルカノイル基などのＣ１−６アシル基など）で保護されているものも含まれる。 The amino acid constituting the peptide of the present invention may be one in which the side chain is modified with an arbitrary substituent. Although a substituent is not specifically limited, For example, a fluorine atom, a chlorine atom, a cyano group, a hydroxyl group, a nitro group, an alkyl group, a cycloalkyl group, an alkoxy group, an amino group etc. are mentioned. Furthermore, in the peptide of the present invention, the amino group of the N-terminal methionine residue is protected with a protecting group (for example, a C 1-6 acyl group such as a C 2-6 alkanoyl group such as formyl group or acetyl). A glutamyl group produced by cleavage of the N-terminal side in vivo, pyroglutamine oxidation, a substituent on the side chain of an amino acid in the molecule (for example, —OH, —SH, amino group, imidazole group, indole group) , A guanidino group, and the like) are protected with an appropriate protecting group (for example, a C 1-6 acyl group such as a C 2-6 alkanoyl group such as formyl group or acetyl).
本発明のペプチドは塩を形成していてもよく、その塩としては、例えば、塩酸、硫酸、燐酸、乳酸、酒石酸、マレイン酸、フマル酸、シュウ酸、リンゴ酸、クエン酸、オレイン酸、パルミチン酸などの酸との塩；ナトリウム、カリウム、カルシウムなどのアルカリ金属もしくはアルカリ土類金属の、またはアルミニウムの水酸化物または炭酸塩との塩；トリエチルアミン、ベンジルアミン、ジエタノールアミン、ｔ−ブチルアミン、ジシクロヘキシルアミン、アルギニンなどとの塩などが挙げられる。 The peptide of the present invention may form a salt. Examples of the salt include hydrochloric acid, sulfuric acid, phosphoric acid, lactic acid, tartaric acid, maleic acid, fumaric acid, oxalic acid, malic acid, citric acid, oleic acid, palmitic acid. Salts with acids such as acids; salts with alkali or alkaline earth metals such as sodium, potassium, calcium, or aluminum hydroxides or carbonates; triethylamine, benzylamine, diethanolamine, t-butylamine, dicyclohexylamine And salts with arginine and the like.
〔金属吸着剤およびレアメタル回収方法〕
本発明のペプチドは金属（金属イオン）と結合できる性質を有するため、金属吸着剤として好適に用いることができる。本発明の金属吸着剤の吸着対象金属は、本発明のペプチドに特異的（選択的）に結合可能な金属に限定されず、非特異的に結合可能な金属であってもよい。本発明の金属吸着剤の吸着対象金属としては、例えば、金、銀、銅、亜鉛、白金、パラジウム、コバルト、クロム、マンガン、ニッケルなどが挙げられる。
[Metal adsorbent and rare metal recovery method]
Since the peptide of this invention has the property which can be couple | bonded with a metal (metal ion), it can be used suitably as a metal adsorbent. The metal to be adsorbed by the metal adsorbent of the present invention is not limited to a metal that can specifically (selectively) bind to the peptide of the present invention, and may be a metal that can bind nonspecifically. Examples of the metal to be adsorbed by the metal adsorbent of the present invention include gold, silver, copper, zinc, platinum, palladium, cobalt, chromium, manganese, nickel and the like.
本発明のペプチドは選択的レアメタル結合能を有しているので、レアメタル吸着剤として有用である。レアメタルとしては、例えば、白金、パラジウム、ロジウム、イリジウム、ルテニウム、オスミウム、金、銀、コバルト、クロム、マンガン、ニッケルなどが挙げられる。好ましくはパラジウムおよび／または白金である。 Since the peptide of the present invention has selective rare metal binding ability, it is useful as a rare metal adsorbent. Examples of rare metals include platinum, palladium, rhodium, iridium, ruthenium, osmium, gold, silver, cobalt, chromium, manganese, nickel, and the like. Palladium and / or platinum are preferred.
本発明の金属吸着剤は、本発明のペプチドのみからなるものでもよいが、本発明のペプチド以外のものを含んでもよい。好ましくは、本発明のペプチドが適当な担体に担持された形態の金属吸着剤である。担体は、本発明のペプチドを担持可能なものであれば特に限定されず、公知のペプチド担体から適宜選択して用いることができる。担体の材質は特に限定されず、例えば、紙、木材、プラスチック等が挙げられる。担体の形状は特に限定されず、平板状、球状、糸状等が挙げられる。 The metal adsorbent of the present invention may be composed only of the peptide of the present invention, but may contain other than the peptide of the present invention. Preferably, it is a metal adsorbent in a form in which the peptide of the present invention is supported on a suitable carrier. The carrier is not particularly limited as long as it can carry the peptide of the present invention, and can be appropriately selected from known peptide carriers. The material of the carrier is not particularly limited, and examples thereof include paper, wood, and plastic. The shape of the carrier is not particularly limited, and examples thereof include a flat plate shape, a spherical shape, and a thread shape.
本発明の金属吸着剤を、金属成分を含有する水溶液と接触させることにより、本発明のペプチドが水溶液中の金属イオンと結合し、結合した金属を回収することができる。したがって、本発明は、上記本発明の金属吸着剤と金属成分を含有する水溶液とを接触させる工程を含む金属回収方法を提供する。また、本発明のペプチドは、レアメタルと特異的（選択的）に結合することができるので、回収対象金属をレアメタルとすることが好ましい。レアメタルを回収する場合は、本発明の金属吸着剤とレアメタルを含む金属成分を含有する水溶液とを接触させればよい。回収対象のレアメタルとしては、上記に例示したものが好ましい。 By bringing the metal adsorbent of the present invention into contact with an aqueous solution containing a metal component, the peptide of the present invention binds to metal ions in the aqueous solution, and the bound metal can be recovered. Therefore, this invention provides the metal collection | recovery method including the process which the metal adsorbent of the said invention and the aqueous solution containing a metal component are made to contact. Moreover, since the peptide of this invention can couple | bond with a rare metal specifically (selectively), it is preferable to make a collection object metal into a rare metal. When recovering the rare metal, the metal adsorbent of the present invention may be brought into contact with an aqueous solution containing a metal component containing the rare metal. As the rare metal to be collected, those exemplified above are preferable.
本発明のレアメタル回収方法では、本発明の金属吸着剤とレアメタルを含む金属成分を含有する水溶液とを接触させた後、例えば、遠心分離、ろ過、ｐＨの変化などによりレアメタルが結合した本発明の金属吸着剤を回収し、酵素による加水分解や燃焼によって金属吸着剤を分解消滅させることなどにより本発明の金属吸着剤からレアメタルを分離すればよい。 In the rare metal recovery method of the present invention, after bringing the metal adsorbent of the present invention into contact with an aqueous solution containing a metal component containing a rare metal, the rare metal is bound by, for example, centrifugation, filtration, pH change, etc. What is necessary is just to isolate | separate a rare metal from the metal adsorbent of this invention by collect | recovering a metal adsorbent and decomposing | dissolving a metal adsorbent by enzyme hydrolysis or combustion.
〔レアメタル検出方法〕
本発明者らは、後の実施例で示すように、本発明のペプチドが特定のレアメタルと結合することにより構造変化することを見出した。したがって、本発明は、本発明のペプチドを用いるレアメタル検出方法を提供することができる。すなわち、本発明のレアメタル検出方法は、本発明のペプチドと目的のレアメタルを含有する可能性のある水溶液とを接触させる工程、および、接触後の本発明のペプチドの構造変化を検出する工程を含むものであればよい。本発明のレアメタル検出方法において、本発明のペプチドは、上記本発明の金属吸着剤の形態で使用することが好ましい。ペプチドの構造変化を検出する手段としては、特に限定されないが、例えば、円二色性（ＣＤ）測定、赤外分光（ＩＲ）測定、核磁気共鳴（ＮＭＲ）測定などが挙げられる。
[Rare metal detection method]
The present inventors have found that the structure of the peptide of the present invention is changed by binding to a specific rare metal, as shown in the following examples. Therefore, the present invention can provide a rare metal detection method using the peptide of the present invention. That is, the rare metal detection method of the present invention includes a step of bringing the peptide of the present invention into contact with an aqueous solution that may contain the target rare metal, and a step of detecting a structural change of the peptide of the present invention after contact. Anything is acceptable. In the rare metal detection method of the present invention, the peptide of the present invention is preferably used in the form of the metal adsorbent of the present invention. The means for detecting the structural change of the peptide is not particularly limited, and examples thereof include circular dichroism (CD) measurement, infrared spectroscopy (IR) measurement, and nuclear magnetic resonance (NMR) measurement.
〔レアメタルセンサー〕
本発明のペプチドは特定のレアメタルと結合することにより構造変化するので、特定のレアメタルに対するセンシング素子として用いることができる。本発明のペプチドを用いるセンシング素子と、特定のレアメタルの結合に伴うペプチドの構造変化を他の信号に変換する手段とを組み合わせることにより、特定のレアメタルに対するセンサー（検出器）を提供することができる。
[Rare metal sensor]
Since the structure of the peptide of the present invention is changed by binding to a specific rare metal, it can be used as a sensing element for the specific rare metal. A sensor (detector) for a specific rare metal can be provided by combining a sensing element using the peptide of the present invention and a means for converting the structural change of the peptide accompanying the binding of the specific rare metal into another signal. .
以下、実施例により本発明を詳細に説明するが、本発明はこれらに限定されるものではない。 EXAMPLES Hereinafter, although an Example demonstrates this invention in detail, this invention is not limited to these.
〔実施例１：人工ペプチドの金属イオン結合能の検討〕
（１）ペプチドの合成
以下の４種類のペプチドを、ペプチド合成機（Pioneer, Peptide synthesis System; Applied Biosystems社製）を用いて、Ｆ−ｍｏｃ固相法により合成した。
Ｍ２ＳＡＰ２：ＳＤＰＬＶＮＲＡＳＬＩＧＬＬＨＬＬＬＷＲＭＤＲＬ（配列番号２）
Ｍ２ＳＡＰ３：ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＭＤＲＫ（配列番号３）
Ｍ２ＳＡＰ５：ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＬＥＲＫ（配列番号４）
Ｍ２ＳＡＰ６：ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＡＬＬＬＷＫＭＤＲＫ（配列番号５）
[Example 1: Examination of metal ion binding ability of artificial peptide]
(1) Peptide synthesis The following four types of peptides were synthesized by the F-moc solid phase method using a peptide synthesizer (Pioneer, Peptide synthesis System; Applied Biosystems).
M2SAP2: SDPLVNRASLIGLLLHLLWRMDRL (SEQ ID NO: 2)
M2SAP3: SDPLVRRASLIGLHLLLWKMDRK (SEQ ID NO: 3)
M2SAP5: SDPLVRRASLIGLLLHLLWKLERK (SEQ ID NO: 4)
M2SAP6: SDPLVRRASLIGLALLLLWKMDRK (SEQ ID NO: 5)
（２）実験方法
（２−１）ＣＤ（円二色性）測定
合成した各ペプチドを酢酸バッファー（ｐＨ５．５）にそれぞれ溶解して、３００μＭのペプチド溶液を調製した。このペプチド溶液にコバルト、銅またはパラジウムを含む溶液を添加した。ペプチド溶液のみ（金属非添加）、コバルト添加ペプチド溶液、銅添加ペプチド溶液およびパラジウム添加ペプチド溶液について、それぞれＣＤを測定した。測定には、Ｊａｓｃｏ Ｊ−７２０ ｓｐｅｃｔｒｏ−ｐｏｌａｒｒｉｍｅｔｅｒ（日本分光社製）を使用し、光路長０．１ｍｍのタイコセルを用いて２００μＬのペプチド溶液について測定した。測定条件は、温度２５℃、走査波長２５０ｎｍ〜１９０ｎｍ、データ間隔０．２ｎｍ、走査速度１００ｎｍ／ｍｉｎ、レスポンス２ｓｅｃ、 バンド幅１ｎｍ、 感度１０ｍｄｅｇ、積算回数８回とした。
(2) Experimental Method (2-1) CD (Circular Dichroism) Measurement Each synthesized peptide was dissolved in an acetate buffer (pH 5.5) to prepare a 300 μM peptide solution. A solution containing cobalt, copper or palladium was added to the peptide solution. CD was measured for the peptide solution only (no metal added), the cobalt-added peptide solution, the copper-added peptide solution, and the palladium-added peptide solution. For the measurement, Jasco J-720 spectro-polarimeter (manufactured by JASCO Corporation) was used, and 200 μL of the peptide solution was measured using a Tyco cell having an optical path length of 0.1 mm. The measurement conditions were a temperature of 25 ° C., a scanning wavelength of 250 nm to 190 nm, a data interval of 0.2 nm, a scanning speed of 100 nm / min, a response of 2 sec, a bandwidth of 1 nm, a sensitivity of 10 mdeg, and an integration count of 8 times.
（２−２）ＩＴＣ測定（等温滴定熱測定）
合成した各ペプチドを酢酸バッファー（ｐＨ５．５）にそれぞれ溶解して、３００μＭのペプチド溶液を調製した。測定には、ＶＰ−ＩＴＣ Ｍｉｃｒｏ Ｃａｌｏｒｉｍｅｔｅｒ（MicroCal社製）を使用した。セルに１．５ｍＬのペプチド溶液を入れ、撹拌しながら銅イオン溶液またはパラジウムイオン溶液を滴定した。得られた発熱量の変化を解析して結合定数を算出した。
(2-2) ITC measurement (isothermal titration heat measurement)
Each synthesized peptide was dissolved in an acetate buffer (pH 5.5) to prepare a 300 μM peptide solution. For the measurement, VP-ITC Micro Calorimeter (manufactured by MicroCal) was used. A 1.5 mL peptide solution was placed in the cell, and a copper ion solution or a palladium ion solution was titrated while stirring. The coupling constant was calculated by analyzing the change in the calorific value obtained.
（３）結果
（３−１）Ｍ２ＳＡＰ２
Ｍ２ＳＡＰ２のＣＤ測定の結果を図１に、ＩＴＣ測定の結果を図２（Ａ）および（Ｂ）に示した。図１から、Ｍ２ＳＡＰ２は、銅イオンまたはパラジウムイオンを添加することによりこれらの金属と結合してα−へリックスに構造変化することが示された。一方、コバルトイオンを添加した場合は構造変化が生じないことが示された。示していないが、他の金属（鉄イオン、ニッケルイオン等）を添加した場合も構造変化が生じなかった。この結果から、Ｍ２ＳＡＰ２は、銅およびパラジウムと選択的に結合することが明らかとなった。図２（Ａ）および（Ｂ）に示した発熱量の変化に基づいて得られた結合常数（表１参照）から、Ｍ２ＳＡＰ２の銅およびパラジウムに対する結合能は同程度であった。
(3) Result (3-1) M2SAP2
The results of CD measurement of M2SAP2 are shown in FIG. 1, and the results of ITC measurement are shown in FIGS. 2 (A) and (B). From FIG. 1, it was shown that M2SAP2 binds to these metals by addition of copper ions or palladium ions and changes its structure to α-helix. On the other hand, it was shown that no structural change occurred when cobalt ions were added. Although not shown, the structural change did not occur when other metals (iron ion, nickel ion, etc.) were added. From this result, it was revealed that M2SAP2 selectively binds to copper and palladium. From the binding constants (see Table 1) obtained based on the changes in the calorific values shown in FIGS. 2A and 2B, the binding capacities of M2SAP2 to copper and palladium were comparable.
（３−２）Ｍ２ＳＡＰ３
Ｍ２ＳＡＰ３のＣＤ測定の結果を図３に、ＩＴＣ測定の結果を図４（Ａ）および（Ｂ）に示した。図３から、Ｍ２ＳＡＰ３は、銅イオンまたはパラジウムイオンを添加することによりこれらの金属と結合してα−へリックスに構造変化することが示された。一方、コバルトイオンを添加した場合は構造変化が生じないことが示された。示していないが、他の金属（鉄イオン、ニッケルイオン等）を添加した場合も構造変化が生じなかった。この結果から、Ｍ２ＳＡＰ３は、銅およびパラジウムと選択的に結合することが明らかとなった。図４（Ａ）および（Ｂ）に示した発熱量の変化に基づいて得られた結合常数（表１参照）から、Ｍ２ＳＡＰ３の銅およびパラジウムに対する結合能は同程度であった。
(3-2) M2SAP3
The results of CD measurement of M2SAP3 are shown in FIG. 3, and the results of ITC measurement are shown in FIGS. 4 (A) and 4 (B). From FIG. 3, it was shown that M2SAP3 binds to these metals by adding copper ions or palladium ions, and changes its structure into an α-helix. On the other hand, it was shown that no structural change occurred when cobalt ions were added. Although not shown, the structural change did not occur when other metals (iron ion, nickel ion, etc.) were added. From this result, it was revealed that M2SAP3 selectively binds to copper and palladium. From the binding constants (see Table 1) obtained based on the changes in the calorific values shown in FIGS. 4A and 4B, the binding capacities of M2SAP3 to copper and palladium were comparable.
（３−３）Ｍ２ＳＡＰ５
Ｍ２ＳＡＰ５のＣＤ測定の結果を図５に、ＩＴＣ測定の結果を図６（Ａ）および（Ｂ）に示した。図５から、Ｍ２ＳＡＰ３は、パラジウムイオンを添加することによりこれと結合してα−へリックスに構造変化することが示された。一方、銅イオンまたはコバルトイオンを添加した場合は構造変化が生じないことが示された。示していないが、他の金属（鉄イオン、ニッケルイオン等）を添加した場合も構造変化が生じなかった。この結果から、Ｍ２ＳＡＰ５は、パラジウムと選択的に結合することが明らかとなった。図６（Ａ）および（Ｂ）に示した発熱量の変化に基づいて得られた結合常数（表１参照）から、Ｍ２ＳＡＰ５のパラジウムに対する結合能は、銅に対する結合能の約４倍であった。なお、パラジウムに対する結合能がＭ２ＳＡＰ３と比して約２倍向上している点で、より有用性が高い。
(3-3) M2SAP5
The results of CD measurement of M2SAP5 are shown in FIG. 5, and the results of ITC measurement are shown in FIGS. 6 (A) and 6 (B). From FIG. 5, it was shown that M2SAP3 was combined with this by adding palladium ion and changed its structure into an α-helix. On the other hand, it was shown that no structural change occurred when copper ions or cobalt ions were added. Although not shown, the structural change did not occur when other metals (iron ion, nickel ion, etc.) were added. From this result, it was revealed that M2SAP5 selectively binds to palladium. From the binding constant (see Table 1) obtained based on the change in the calorific value shown in FIGS. 6A and 6B, the binding ability of M2SAP5 to palladium was about four times that of copper. . In addition, it is more useful in that the binding ability to palladium is improved by about 2 times compared to M2SAP3.
（３−４）Ｍ２ＳＡＰ６
Ｍ２ＳＡＰ６のＣＤ測定の結果を図７に、ＩＴＣ測定の結果を図８（Ａ）および（Ｂ）に示した。図７から、Ｍ２ＳＡＰ６は、パラジウムイオンを添加することによりこれと結合してα−へリックスに構造変化することが示された。一方、銅イオンまたはコバルトイオンを添加した場合は構造変化が生じないことが示された。示していないが、他の金属（鉄イオン、ニッケルイオン等）を添加した場合も構造変化が生じなかった。この結果から、Ｍ２ＳＡＰ６は、パラジウムと選択的に結合することが明らかとなった。図８（Ａ）および（Ｂ）に示した発熱量の変化に基づいて得られた結合常数（表１参照）から、Ｍ２ＳＡＰ６のパラジウムに対する結合能は、銅に対する結合能の約４倍であった。なお、パラジウムに対する結合能がＭ２ＳＡＰ３と比して約４倍向上している点で、より有用性が高い。
(3-4) M2SAP6
The results of CD measurement of M2SAP6 are shown in FIG. 7, and the results of ITC measurement are shown in FIGS. 8 (A) and 8 (B). From FIG. 7, it was shown that M2SAP6 was combined with this by adding palladium ions and changed in structure to an α-helix. On the other hand, it was shown that no structural change occurred when copper ions or cobalt ions were added. Although not shown, the structural change did not occur when other metals (iron ion, nickel ion, etc.) were added. From this result, it was revealed that M2SAP6 selectively binds to palladium. From the binding constant (see Table 1) obtained based on the change in the calorific value shown in FIGS. 8A and 8B, the binding capacity of M2SAP6 to palladium was about 4 times that of copper. . In addition, usefulness is higher in that the binding ability to palladium is improved by about 4 times compared to M2SAP3.
〔実施例２：ペプチド塗工紙のＰｄイオン吸着能の検討〕
（１）ペプチド塗工紙の作製
原紙として、薄葉紙１４ｇ／ｍ２（５０ｍｍ×５０ｍｍ）を用いた。ペプチド塗工液（原液）として、バインダー樹脂（２５％品）４０ｍｇにＭ２ＳＡＰ５を１０ｍｇ添加して攪拌混合したもの（バインダー樹脂（固形量）：ペプチド（固形量）＝１：１）を用いた。ペプチド塗工液の入ったシャーレの中に薄葉紙を入れて含浸させ、その後オーブン乾燥機にて１００℃で１０分間乾燥を行った。ペプチド塗工液（原液）を水で希釈して濃度を調整することにより、塗工量が２ｇ／ｍ２（ペプチド１ｇ／ｍ２）の塗工紙および１ｇ／ｍ２（ペプチド０．５ｇ／ｍ２）の塗工紙の２種類を作製した。
[Example 2: Examination of Pd ion adsorption ability of peptide-coated paper]
(1) Production of peptide-coated paper Thin paper 14 g / m 2 (50 mm × 50 mm) was used as the base paper. As a peptide coating solution (stock solution), 10 mg of M2SAP5 was added to 40 mg of binder resin (25% product) and mixed by stirring (binder resin (solid amount): peptide (solid amount) = 1: 1). A thin paper was placed in a petri dish containing the peptide coating solution and impregnated, and then dried in an oven dryer at 100 ° C. for 10 minutes. By adjusting the concentration by diluting the peptide coating solution (stock solution) with water, the coating amount is 2 g / m 2 (peptide 1 g / m 2 ) and 1 g / m 2 (peptide 0.5 g / peptide). Two types of m 2 ) coated paper were prepared.
（２）Ｐｄイオン吸着試験
パラジウム標準液（１０００ｐｐｍ）が５ｍｌ入ったシャーレに、２５ｍｍ×２５ｍｍ角の塗工紙を４時間含浸させ、パラジウムイオンを吸着させた。その後、残液のパラジウムイオン濃度を原子吸光分光光度計を用いて測定し、初期濃度との差を吸着量とした（ｎ＝２）。
結果を図９および表２に示した。図９は、４時間含浸後の薄葉紙の写真であり、（Ａ）が薄葉紙１４ｇ／ｍ２、（Ｂ）が薄葉紙１４ｇ／ｍ２＋ペプチド塗工液２ｇ／ｍ２、（Ｃ）が薄葉紙１４ｇ／ｍ２＋ペプチド塗工液１ｇ／ｍ２の写真である。図９からわかるように、薄葉紙の着色の程度は（Ｂ）＞（Ｃ）＞（Ａ）であった。また、表２に示したように、薄葉紙に本発明のペプチドを塗工することでパラジウムイオンの吸着量が用量依存的に増加した。また、ペプチド塗工紙作製における原料ペプチドの歩留まりを１００％と仮定した場合、ペプチド１ｇあたりのパラジウムイオン吸着量は約９０〜約１３５ｍｇ／ｇと推定された。
(2) Pd ion adsorption test A petri dish containing 5 ml of a palladium standard solution (1000 ppm) was impregnated with a 25 mm × 25 mm square coated paper for 4 hours to adsorb palladium ions. Thereafter, the palladium ion concentration in the residual liquid was measured using an atomic absorption spectrophotometer, and the difference from the initial concentration was taken as the adsorption amount (n = 2).
The results are shown in FIG. FIG. 9 is a photograph of thin paper after impregnation for 4 hours, (A) is thin paper 14 g / m 2 , (B) is thin paper 14 g / m 2 + peptide coating solution 2 g / m 2 , (C) is thin paper 14 g. It is a photograph of / m 2 + peptide coating solution 1 g / m 2 . As can be seen from FIG. 9, the degree of coloring of the thin paper was (B)>(C)> (A). Moreover, as shown in Table 2, the amount of palladium ion adsorbed increased in a dose-dependent manner by applying the peptide of the present invention to thin paper. Further, assuming that the yield of the starting peptide in peptide-coated paper production was 100%, the palladium ion adsorption amount per 1 g of peptide was estimated to be about 90 to about 135 mg / g.
なお本発明は上述した各実施形態および実施例に限定されるものではなく、請求項に示した範囲で種々の変更が可能であり、異なる実施形態にそれぞれ開示された技術的手段を適宜組み合わせて得られる実施形態についても本発明の技術的範囲に含まれる。また、本明細書中に記載された学術文献および特許文献の全てが、本明細書中において参考として援用される。 The present invention is not limited to the above-described embodiments and examples, and various modifications are possible within the scope shown in the claims, and technical means disclosed in different embodiments are appropriately combined. The obtained embodiment is also included in the technical scope of the present invention. Moreover, all the academic literatures and patent literatures described in this specification are incorporated herein by reference.
Claims (11)
（１）ＳＤＰＬＶＸ１ＲＡＳＬＩＧＬＬＸ２ＬＬＬＷＸ３Ｘ４Ｘ５ＲＸ６（配列番号１）
（Ｘ１は親水性アミノ酸、Ｘ２はＨまたはＡ、Ｘ３はＲまたはＫ、Ｘ４はＭまたは脂肪族アミノ酸、Ｘ５はＤまたはＥ、Ｘ６は任意のアミノ酸を表す。） A peptide having the following amino acid sequence (1) and having 100 or fewer amino acid residues.
(1) SDPLVX 1 RASLIGLLX 2 LLLWX 3 X 4 X 5 RX 6 (SEQ ID NO: 1)
(X 1 represents a hydrophilic amino acid, X 2 represents H or A, X 3 represents R or K, X 4 represents M or an aliphatic amino acid, X 5 represents D or E, and X 6 represents any amino acid.)
（２）ＳＤＰＬＶＮＲＡＳＬＩＧＬＬＨＬＬＬＷＲＭＤＲＬ（配列番号２）
（３）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＭＤＲＫ（配列番号３） The peptide according to claim 2, wherein the amino acid sequence (1) is the following amino acid sequence (2) or (3).
(2) SDPLVNRASLIGLLLHLLWRMDRL (SEQ ID NO: 2)
(3) SDPLVRRASLIGLLLHLLWKMDRK (SEQ ID NO: 3)
（４）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＨＬＬＬＷＫＬＥＲＫ（配列番号４）
（５）ＳＤＰＬＶＲＲＡＳＬＩＧＬＬＡＬＬＬＷＫＭＤＲＫ（配列番号５） The peptide according to claim 2, wherein the amino acid sequence (1) is the following amino acid sequence (4) or (5).
(4) SDPLVRRASLIGLLLHLLWKLERK (SEQ ID NO: 4)
(5) SDPLVRRASLIGLALLLLWKMDRK (SEQ ID NO: 5)
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Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013227281A (en) * | 2012-03-26 | 2013-11-07 | Panasonic Corp | Peptide capable of binding to gold |
| JP2013231024A (en) * | 2012-04-04 | 2013-11-14 | Panasonic Corp | Peptide capable for binding to carbon |
| JP2013234170A (en) * | 2012-04-10 | 2013-11-21 | Panasonic Corp | Peptide capable of being bound to rhodium |
| JP2013234171A (en) * | 2012-04-11 | 2013-11-21 | Panasonic Corp | Peptide capable of being bound to iridium |
| JP2016047810A (en) * | 2014-08-26 | 2016-04-07 | 株式会社デンソー | Peptide, rare earth element recovering material, and recovering method for rare earth elements |
| JP2016088846A (en) * | 2014-10-29 | 2016-05-23 | 株式会社豊田中央研究所 | Rare earth trapping material and application thereof |
| JP2016117664A (en) * | 2014-12-19 | 2016-06-30 | 株式会社豊田中央研究所 | Separation method of rare earth ion |
| WO2017213153A1 (en) * | 2016-06-06 | 2017-12-14 | Shibaura Institute Of Technology | A novel peptide and use thereof |
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Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6160699A (en) * | 1984-08-31 | 1986-03-28 | Agency Of Ind Science & Technol | Novel cyclic octapeptide, its preparation, and extracting and separating agent comprising it as component |
| JPH10338700A (en) * | 1997-06-09 | 1998-12-22 | Kanegafuchi Chem Ind Co Ltd | New peptide compound |
| JP2003284556A (en) * | 1999-11-19 | 2003-10-07 | Toyota Motor Corp | Gene expressing protein capable of capturing metal |
| JP2005503798A (en) * | 2001-09-06 | 2005-02-10 | ロジャー・エイ・エイシー | Methods associated with metal binding proteins |
| JP2008521431A (en) * | 2004-12-02 | 2008-06-26 | シーエスアイアール | Gram-positive bacterial cells containing a disrupted flagellin gene, flagellin-based fusion protein and use in removal of metal ions from liquids |
-
2012
- 2012-03-05 JP JP2012047585A patent/JP5943463B2/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6160699A (en) * | 1984-08-31 | 1986-03-28 | Agency Of Ind Science & Technol | Novel cyclic octapeptide, its preparation, and extracting and separating agent comprising it as component |
| JPH10338700A (en) * | 1997-06-09 | 1998-12-22 | Kanegafuchi Chem Ind Co Ltd | New peptide compound |
| JP2003284556A (en) * | 1999-11-19 | 2003-10-07 | Toyota Motor Corp | Gene expressing protein capable of capturing metal |
| JP2005503798A (en) * | 2001-09-06 | 2005-02-10 | ロジャー・エイ・エイシー | Methods associated with metal binding proteins |
| JP2008521431A (en) * | 2004-12-02 | 2008-06-26 | シーエスアイアール | Gram-positive bacterial cells containing a disrupted flagellin gene, flagellin-based fusion protein and use in removal of metal ions from liquids |
Non-Patent Citations (3)
| Title |
|---|
| JPN6016003993; Ｃｕｒｒｅｎｔ Ｏｐｉｎｉｏｎ ｉｎ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ Ｖｏｌ．２２, 2011, ｐ．４２７-４３３ * |
| JPN6016003994; Ｊｏｕｒｎａｌ ｏｆ Ｃｈｒｏｍａｔｏｇｒａｐｈｙ Ａ Ｖｏｌ．１２１７, 2010, ｐ．５９４０-５９４９ * |
| JPN6016003995; Ｉｎｔｅｒｎａｔｉｏｎａｌ Ｂｉｏｄｅｔｅｒｉｏｒａｔｉｏｎ ＆ Ｂｉｏｄｅｇｒａｄａｔｉｏｎ Ｖｏｌ．６０, 2007, ｐ．９６-１０２ * |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013227281A (en) * | 2012-03-26 | 2013-11-07 | Panasonic Corp | Peptide capable of binding to gold |
| JP2013231024A (en) * | 2012-04-04 | 2013-11-14 | Panasonic Corp | Peptide capable for binding to carbon |
| JP2013234170A (en) * | 2012-04-10 | 2013-11-21 | Panasonic Corp | Peptide capable of being bound to rhodium |
| JP2013234171A (en) * | 2012-04-11 | 2013-11-21 | Panasonic Corp | Peptide capable of being bound to iridium |
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| JP2016088846A (en) * | 2014-10-29 | 2016-05-23 | 株式会社豊田中央研究所 | Rare earth trapping material and application thereof |
| JP2016117664A (en) * | 2014-12-19 | 2016-06-30 | 株式会社豊田中央研究所 | Separation method of rare earth ion |
| US10400310B2 (en) | 2014-12-19 | 2019-09-03 | Kabushiki Kaisha Toyota Chuo Kenkyusho | Method for separation of rare earth ion |
| WO2017213153A1 (en) * | 2016-06-06 | 2017-12-14 | Shibaura Institute Of Technology | A novel peptide and use thereof |
| JP2017216919A (en) * | 2016-06-06 | 2017-12-14 | 学校法人 芝浦工業大学 | Novel peptide and method for using the same |
| US11168113B2 (en) | 2016-06-06 | 2021-11-09 | Shibaura Institute Of Technology | Peptide and use thereof |
| CN112113998A (en) * | 2020-09-23 | 2020-12-22 | 上海理工大学 | Method for exploring interaction between metal ions and biological small molecules by isothermal titration quantitative calorimetry |
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