Eine neue enzymatische Peptidsynthese. 1. Mitteilung

Brenner, M.; Müller, H.; Pfister, R.

doi:10.1002/hlca.19500330322

Cited by 101 publications

(24 citation statements)

References 28 publications

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“…The first reports by Brenner et al in 1950 showed the oligomerization of threonine and methionine esters by α-chymotrypsin [11][12][13]. Others used bovine lung proteinase [14], ficin and Cathepsin-C [15] a protease from Streptomyces sp.…”

Section: Introductionmentioning

confidence: 99%

Papain Catalyzed (co)Oligomerization of α-Amino Acids

Schwab¹,

Kloosterman²,

Konieczny³

et al. 2012

Polymers

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Four hydrophobic amino acids (Leu, Tyr, Phe, Trp) were oligomerized by the protease papain in homo-oligomerization, binary co-oligomerization and ternary co-oligomerization. After 24 h, solid polydisperse reaction products of the homo-oligomerization were obtained in yields ranging from 30-80% by weight. A DP avg was calculated based on MALDI-ToF MS results using the ion counts for the chains in the product. Based on the DP avg and the yield of the homo-oligomerization it was determined that the amino acids can be ranked according to reactivity in the order: Tyr > Leu > Phe > Trp. Thermal degradation of the homo-oligomers shows two degradation steps: at 178-239 °C and at 300-330 °C. All the products left a significant amount of char ranging from 18-57% by weight at 800 °C. Binary co-oligomers were obtained as a polydisperse precipitate with a compositional distribution of the chains. Both the compositional and chain length distribution are calculated from MALDI-ToF mass spectra. By comparing the amount of each amino acid present in the chains it was determined that the amino acids are incorporated with a preference: Leu > Tyr > Phe > Trp. Ternary co-oligomers were also obtained as a precipitate and analyzed by MALDI-ToF MS. The compositional distribution and the chain length distribution were calculated from the MALDI-ToF data. The quantity of every amino acid in the chains was determined. Also determined was the influence on the DP avg when the oligomers were compared with corresponding binary co-oligomers. From the combined results it was concluded that in the co-oligomerization of three amino acids the reactivity preference is Leu > Tyr > Phe > Trp. OPEN ACCESSPolymers 2012, 4 711Thermal degradation of all the co-oligomers showed a weight loss of 2 wt% before the main oligomer degradation step at 300-325 °C.

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Section: Introductionmentioning

confidence: 99%

Papain Catalyzed (co)Oligomerization of α-Amino Acids

Schwab¹,

Kloosterman²,

Konieczny³

et al. 2012

Polymers

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“…Methyl, [49,58] ethyl, [44,46,60] isopropyl [23,24] Proteinase I, [49] papain (3.4-6), [58,60] α-chymotrypsin, [23,24] proteinase K (2-7), [44] bromelain (7.5-8.3) [46] l-Threonine…”

Section: Materials and General Protocolsmentioning

confidence: 99%

“…Ethyl, [49] isopropyl [23,24] Proteinase I, [49] papain (5)(6)(7)(8)(9)(10)(11)(12)(13)(14), [60,67,68] α-chymotrypsin [23,24] l-Lysine…”

Section: Materials and General Protocolsmentioning

confidence: 99%

“…[22] In contrast, the enzymatic synthesis of polypeptides was initially developed to obtain di-, tri-, and oligopeptides. [23][24][25][26][27] Enzymes categorized as hydrolases digest covalent bonds, such as the amide and ester bonds in living systems, and have been exploited to chemically construct various organic materials. Proteases generally hydrolyze the amide bonds in proteins (polypeptides), and this reaction proceeds in a reversible manner.…”

Section: Introductionmentioning

confidence: 99%

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Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Tsuchiya

Numata

2017

Macromolecular Bioscience

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Polypeptides inspired by the natural functional and structural proteins present in living systems are promising materials for various fields in terms of their versatile functionality and physical properties. Designing and synthesizing mimetic sequences of specific peptide motifs in proteins are important for exploring the functionality of natural proteins. Chemoenzymatic polymerization, which utilizes aminolysis (i.e., the reverse reaction of hydrolysis catalyzed by proteases), is a useful technique for synthesizing artificial polypeptide materials and has several advantages, including facile synthesis protocols, environmental friendliness, scalability, and atom economy. In this review, recent progress in chemoenzymatic polypeptide synthesis for the production of functional and structural materials for various applications is summarized in conjunction with the current status of technical challenges in the field.

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“…In den 1 3 C-und 1 H -N M RSpektren weisen die R esonanzsignale der Benzoylg ruppe eine große negative K oordinationsver- [29] w urden wie in d er L iteratu r beschrieben erhalten. D ,L-2-(3-Thienyl)glycinm ethylester [30], N-Benzoyl-D ,L-2(3-Thienyl)glycin [31] und dessen M e thylester [32] 136,5, 127,8, 126,9, 124,5 (C 4H 3S), 167,1 (C O ), 133,7, 132,0, 128,6, 128,0 (C 6H 5). …”

Section: Etallorganische Komplexe M It N-geschiitztem 2-(3-thienyl)unclassified

Metallkomplexe mit biologisch wichtigen Liganden, LXXIV [1]. Metallorganische Verbindungen von 2-(3-Thienyl)glycin und dessen Derivaten / Metal Complexes with Biologically Important Ligands, LXXIV [1]. Organometallic Compounds of 2-(3-Thienyl)glycine and Derivatives thereof

Schuhmann

Robl

Beck

1994

Zeitschrift Für Naturforschung B

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N.O-Chelate complexes of R,S-2-(3-thienyl)glycinate (L) have been obtained: ML2 (M = Ni, Cu), (n-Bu3P)(Cl)M(L) (M = Pd. Pt), (η3-C3H5)Pd(L), C6H4CH,CHNMe2Pd(L), (η6-p-cymene)(Cl)Ru(L), (η5-C5Me5)(Cl)M(L) (M = Rh, Ir) and (η5-C5H5)(OC)2Mo(L). The methyl ester of R,S-2-(3-thienvl)glycine (L') forms the complexes trans-CT2PdL′2, cis- Cl2Pt(L')2, (η-Bu3P)(Cl2)M(L') (M = Pd, Pt) and (η5-C5Me5)(Cl)2M(L') (M = Rh, Ir) in which the ligand L' is coordinated through the amino group. The structures of (η3-C3H5)Pd(L) and of (η5-C5Me5)(Cl2)Ir(L') have been determined by X-ray diffraction. N- Benzoyl-2-(3-thienylglycine methyl ester reacts with Cr(CO)6 to yield a tricarbonyl complex with an η6-coordinated phenyl group. N-Benzoyl-R,S-2-(3-thienyl)glycinate (L") and (η5- C5H5)2TiCl2 give the diastereoisomers [(η5-C5H5)2Ti(R-L")(R-L")2/(η5-C5H5)2Ti(S-L") (S-L")] and (η5-C5H5)2Ti(R-L")(S-L") with Ti-O-bonds.

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Eine neue enzymatische Peptidsynthese. 1. Mitteilung

Abstract: Die Ester des Methionins und einiger anderer spezifischer Aminosäuren reagieren in Gegenwart von Wasser und käuflichen Präparaten von kristallisiertem Chymotrypsin unter Bildung von Peptiden.

Cited by 101 publications

References 28 publications

Papain Catalyzed (co)Oligomerization of α-Amino Acids

Papain Catalyzed (co)Oligomerization of α-Amino Acids

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Metallkomplexe mit biologisch wichtigen Liganden, LXXIV [1]. Metallorganische Verbindungen von 2-(3-Thienyl)glycin und dessen Derivaten / Metal Complexes with Biologically Important Ligands, LXXIV [1]. Organometallic Compounds of 2-(3-Thienyl)glycine and Derivatives thereof

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