Chemoenzymatic synthesis of peptides is a green and clean chemical reaction that offers high yields without using organic synthesis and serves as an alternative to traditional peptide synthesis methods. This report describes the chemoenzymatic synthesis of oligo(L-phenylalanine) mediated by proteinase K from Tritirachium album, which is one of the most widely used proteases in molecular biological studies. The synthesized linear oligo-phenylalanine showed a unique self-assembly in aqueous solutions. To further functionalize linear oligo(L-phenylalanine) as a low-molecular-weight gelator, it was cosynthesized with tris(2-aminoethyl)amine to obtain star-oligo(L-phenylalanine), which was bioconjugated to demonstrate its self-assembly into fluorescent fibers. The self-assembled fibers of star-oligo(L-phenylalanine) formed fibrous networks with various branching ratios, which depended on the molecular weights and molecular aspect ratios of star-oligo(L-phenylalanine). This is the first study to demonstrate that proteinase K is a suitable enzyme for chemoenzymatic cosynthesis of oligopeptides and star-shaped heteropeptides.
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http://dx.doi.org/10.1021/bm4009974 | DOI Listing |
Carbohydr Polym
March 2025
Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea; Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea; Center for Agricultural Microorganism and Enzyme, Seoul National University, Seoul 08826, Republic of Korea; Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Republic of Korea. Electronic address:
Chitosan (CS) is a versatile polysaccharide with numerous inherent biological activity, while the lack of amphiphilicity limits its application in emulsion-based systems. In this study, erythorbyl myristate (EM) with interfacial activity was chemically modified to 5-O-succinyl EM (EMS) and grafted onto CS to improve the emulsifying properties. The grafting reaction was conducted by the catalysis of protease, with the progress of the reaction monitored by HPLC analysis and UV absorbance measurement.
View Article and Find Full Text PDFOrg Lett
January 2025
Biomimetic Catalysis, Catalysis Research Center, TUM School of Natural Sciences, Technical University of Munich, Lichtenbergstrasse 4, 85748 Garching, Germany.
Inspired by natural cryptic halogenation in -bond formation, this study developed a synthetic approach combining biocatalytic bromination with transition-metal-catalyzed cross-coupling. Using the cyanobacterial VHPO, a robust and sustainable bromination-arylation cascade was created. Genetic modifications allowed enzyme immobilization, enhancing the compatibility between biocatalysis and chemocatalysis.
View Article and Find Full Text PDFProteoglycan Res
October 2024
Department of Biochemistry and Physiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Hyaluronan (HA; [-3-GlcNAc-1-beta-4-GlcA-1-beta] ), an essential matrix polysaccharide of vertebrates and the molecular camouflage coating in certain pathogens, is polymerized by "HA synthase" (HAS) enzymes. Three HAS classes have been identified with biotechnological utility, but only the Class II PmHAS from Type A has been useful for preparation of very defined HA polymers in vitro. Two general chemoenzymatic strategies with different size products are possible: (1) repetitive step-wise extension reactions by sequential addition of a single monosaccharide from a donor UDP-sugar onto an acceptor (or "primer") comprised of a short glycosaminoglycan chain (e.
View Article and Find Full Text PDFBiochemistry
January 2025
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
The pathogen-associated -glucosyltransferase IroB is involved in the biosynthesis of salmochelins, -glucosylated derivatives of enterobactin (Ent), which is a triscatecholate siderophore of enteric bacteria including and . Here, we reassess the ability of IroB to -glucosylate non-native triscatecholate mimics of Ent, which may have utility in the design and development of siderophore-based therapeutics and diagnostics. We establish TRENCAM (TC) and MECAM (MC), synthetic Ent analogs with tris(2-aminoethyl)amine- or mesitylene-derived backbones replacing the trilactone core of Ent, respectively, and their monoglucosylated congeners as substrates of IroB.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
December 2024
TU Dresden: Technische Universitat Dresden, Faculty of Chemistry and Food Chemistry, Bergstraße 66, 01069, Dresden, GERMANY.
Polycyclic tetramate macrolactams (PoTeMs) represent a growing class of bioactive natural products that are derived from a common tetramate polyene precursor, lysobacterene A, produced by an unusual bacterial iterative polyketide synthase (PKS) / non-ribosomal peptide synthetase (NRPS). The structural and functional diversity of PoTeMs is biosynthetically elaborated from lysobacterene A by pathway-specific cyclizing and modifying enzymes. This results in diverse core structure decoration and cyclization patterns.
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