Simplifying alternating peptide synthesis by protease-catalyzed dipeptide oligomerization

Xu, Qin; Khuong, Anne C.; Yu, Zheng; Du, Wenzhe; Decatur, John; Gross, Richard A.

doi:10.1039/c2cc36381j

Cited by 34 publications

(50 citation statements)

References 39 publications

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“…43 Alternating oligopeptides were synthesized by papain-mediated catalysis using the dipeptide monomer, alanine-glycine ethyl ester. 44 Papain-catalyzed oligomerization of L-lysine protected at the side chain with a tert-butoxycarbonyl or carboxybenzyl group ensures a higher yield and a simpler purification process owing to the precipitation-driven reaction derived from the hydrophobicity of the protected group. 45 Thus, papain is powerful, and the most-studied protease for chemoenzymatic synthesis of various types of peptides.…”

Section: Poly(amino Acid) As An Eco-friendly Materialsmentioning

confidence: 99%

Poly(amino acid)s/polypeptides as potential functional and structural materials

Numata

2015

Polym J

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Poly(amino acids) and polypeptides have the potential to contribute significantly to a biomass-based and sustainable society, due to their biomass origin, functionality, and unique physical properties. To realize amino acid-based polymers as eco-friendly alternatives for petroleum materials, the synthesis of poly(amino acid)s/polypeptides through an environmentally friendly process is needed. In this focus review, the author summarizes the recent progress of chemo-enzymatic polymerization, which is a green and atom-economical reaction that provides new insight into the design of materials from polypeptides. Additionally, polypeptides can be designed to serve as functional and structural materials. The use of peptides as carriers of nucleic acids for delivery into target cells and organelles is one important application of such functional materials. Studies on polypeptides as structural materials are also reviewed. POLY(AMINO ACID) AS AN ECO-FRIENDLY MATERIALEco-friendly polymeric materials have been designed and processed primarily from bio-based polyesters such as poly(hydroxyalkanoate) 1 and poly(lactic acid), 2,3 due to their plasticity, excellent workability, and biomass origin. 4-12 Poly(hydroxyalkanoate) has several advantages such as the ability to be directly synthesized from various types of biomass, including lignin and carbon dioxide, 13-17 and excellent biodegradability. 18,19 However, because of a lack of toughness, this biopolyester has limited use and application. Development of an engineered biopolymer such as a biomass-derived polyamide is an emerging interest in the field of sustainable chemistry and materials engineering. Biopolyamides (for example, nylon 4) have been investigated as candidates for biomass-based engineering plastics, but their narrow processing window for thermo-forming currently prevents them from being considered for practical purposes. 20 Natural high-performance materials, including spider silk and mussel-derived adhesive (Figure 1), are mainly composed of poly(amino acid)s and a small amount of short peptides, suggesting that poly(amino acid)s could serve as an alternative to the petroleum-derived polymers in support of a sustainable society. Although spider dragline silk is a benchmark in terms of tough materials, scientific and technological advances still cannot produce an artificial dragline silk. To create and develop biomass-based tough polymers like this silk, the synthesis and design of materials from poly(amino acid)s is being investigated.A poly(amino acid) is a polymer composed of amino acids as monomeric units. Structural and functional proteins, polypeptides, peptides and polymers derived from amino acids, that is, poly(β-alanine) and ε-poly(lysine), are classified as poly(amino acid)s. The use of poly(amino acid)s as functional materials has been widely studied, resulting in the development of polypeptides that are bioactive and that can have biological applications such as in tissue engineering, regenerative medicine and drug/gene delivery systems. Poly(amin...

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Section: Poly(amino Acid) As An Eco-friendly Materialsmentioning

confidence: 99%

Poly(amino acid)s/polypeptides as potential functional and structural materials

Numata

2015

Polym J

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“…In contrast, CPDY is characterized as an exopeptidase that typically cleaves only amide bonds at C-termini. Therefore, CPDY-catalyzed polymerization avoids the hydrolysis of the polypeptide backbones of pre-existing polypeptides, resulting in efficient suppression of the broadening of the molecular weight distribution of the products that Methyl, [49,54] ethyl, [50][51][52][53][54][55][56] benzyl [54] Proteinase I, [49] papain (13)(14)(15)(16)(17)(18) [50][51][52][53][54][55][56] Glycine Methyl, [54] ethyl, [49,51,54,55] benzyl [54] Proteinase I, [49] papain (10)(11)(12)(13)(14)(15)(16)(17)(18)(19) [51,54,55] l-Leucine…”

Section: Materials and General Protocolsmentioning

confidence: 99%

“…Gross et al demonstrated that a dipeptide ester, l-alanylglycine ethyl ester (AlaGly-OEt), is a preferable substrate for papain and could be converted into a polypeptide with the strictly alternating sequence poly(Ala-alt-Gly) via chemoenzymatic polymerization. [51] On MALDI-TOF mass spectrometry, the polypeptides obtained from the AlaGly-OEt showed a series of peaks that corresponded to polypeptides containing stoichiometrically equivalent quantities of alternating l-alanine and glycine units. Thus, the use of dipeptide esters as monomers in chemoenzymatic polymerization can yield polypeptides with various types of alternating sequences.…”

Section: Hydrophobic Polypeptides For Structural Materialsmentioning

confidence: 99%

“…A) Chemoenzymatic polymerization of dipeptide ethyl esters yields an alternating polypeptide consisting of Ala and Gly. [51] B) Chemoenzymatic copolymerization of Ala and Gly benzyl esters. [54] www.advancedsciencenews.com www.mbs-journal.de of these esters was thoroughly investigated by screening the effects of the ester groups of monomers, including methyl, ethyl, benzyl, and tert-butyl esters.…”

Section: Hydrophobic Polypeptides For Structural Materialsmentioning

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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“…Among the huge number of commercial enzymes, proteases are of great importance for their extensive applications in detergent, tanning, food processing, silk degumming, medical diagnosis, bioconversion, waste treatment, and peptide synthesis [2][3][4][5]. Currently, proteases have accounted for up to 60% of the total enzyme sales in the global market, in which alkaline proteases represent the largest portion [6].…”

Section: Introductionmentioning

confidence: 99%

A salt, detergent, and solvent tolerant protease from <i>Bacillus</i> sp. B001: Low-cost, easy-purified, and enhanced production by raw material based culture strategy

Wu¹,

Deng²,

Shi³

et al. 2013

ABB

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To enhance the protease production and decrease cost, corn flour and soy peptone were screened as cheap raw materials for the production of extracellular proteases by Bacillus strains. Their compositions in the medium suitable for enzyme production of Bacillus sp. B001 were optimized using statistical experiment designs. Under the optimized conditions, the protease production of Bacillus sp. B001 was stable at the stationary stage and reached to 63,200 U/mL, approximately 1.84-fold increase compared with that using the original medium. These improvements could be attributed to the release of the catabolite repression by crude materials corn flour and soy peptone which contained low level of available nutrients. Additionally, a highly pure protease which displayed excellent stability and compatibility with high salinity, commercial laundry detergents, and organic solvents, was rapidly obtained by two-step procedure involving ammonium sulphate precipitation and anion exchange from the fermentation cultures of B001 in the optimized medium. When the culture method applied to other Bacillus strains, their protease yields were all remarkably increased approximately 2.9 to 8.5 folds. In conclusion, a low-cost, easy-purified, and effective producing strategy using the cheap raw materials was developed here, representing a potential application for protease production in various Industrial processes.

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Simplifying alternating peptide synthesis by protease-catalyzed dipeptide oligomerization

Cited by 34 publications

References 39 publications

Poly(amino acid)s/polypeptides as potential functional and structural materials

Poly(amino acid)s/polypeptides as potential functional and structural materials

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

A salt, detergent, and solvent tolerant protease from <i>Bacillus</i> sp. B001: Low-cost, easy-purified, and enhanced production by raw material based culture strategy

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Simplifying alternating peptide synthesis by protease-catalyzed dipeptide oligomerization

Cited by 34 publications

References 39 publications

Poly(amino acid)s/polypeptides as potential functional and structural materials

Poly(amino acid)s/polypeptides as potential functional and structural materials

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

A salt, detergent, and solvent tolerant protease from &lt;i&gt;Bacillus&lt;/i&gt; sp. B001: Low-cost, easy-purified, and enhanced production by raw material based culture strategy

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A salt, detergent, and solvent tolerant protease from <i>Bacillus</i> sp. B001: Low-cost, easy-purified, and enhanced production by raw material based culture strategy