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Clay Mineral Minerals as a Strategy for Biomolecule Incorporation: Amino Acids Approach.

ABSTRACT: The potential use of amino acids by ruminal microorganisms converting them into microbial protein for ruminants makes it challenging to supplement these nutrients in an accessible form in animals' diets. Several strategies to protect amino acids from ruminal degradation were reported, producing amino acids available for the protein used in the intestine called "bypass." The intercalation of biomolecules in clay mineral minerals has gained notoriety due to its ability to support, protect, transport, physicochemical properties and non-toxicity. This study aimed to investigate the incorporation of L-lysine (Lys), L-methionine (Met), and L-tryptophan (Trp) amino acids in the clay minerals sepiolite (Sep) and Veegum^® (Veg) using the adsorption method. The characterization techniques of X-ray diffraction and infrared spectroscopy indicated the presence of biomolecules in the inorganic matrices. Elemental and thermal analyzes monitored the percentages of incorporated amino acids. They showed better incorporation capacities for Veg, such as Met-Veg < Lys-Veg < Trp-Veg and Lys-Sep < Met-Sep < Trp-Sep for sepiolite, except for the incorporation of Met. Matrices provide a promising alternative for planning the administration of biomolecules, using essential amino acids as models, and may offer an alternative to improve functional diet strategies.

SUBMITTER: Brandao-Lima LC

PROVIDER: S-EPMC8745852 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Synthetic biology holds promise to revolutionize the life sciences and biomedicine via expansion of macromolecular diversity outside the natural chemical space. Use of non-canonical amino acids (ncAAs) via codon reassignment has found diverse applications in protein structure and interaction analysis, introduction of post-translational modifications, production of constrained peptides, antibody-drug conjugates, and novel enzymes. However, simultaneously encoding multiple ncAAs in vivo requires complex engineering and is sometimes restricted by the cell's poor uptake of ncAAs. In contrast the open nature of cell-free protein synthesis systems offers much greater freedom for manipulation and repurposing of the biosynthetic machinery by controlling the level and identity of translational components and reagents, and allows simultaneous incorporation of multiple ncAAs with non-canonical side chains and even backbones (N-methyl, D-, ?-amino acids, ?-hydroxy acids etc.). This review focuses on the two most used Escherichia coli-based cell-free protein synthesis systems; cell extract- and PURE-based systems. The former is a biological mixture with >500 proteins, while the latter consists of 38 individually purified biomolecules. We delineate compositions of these two systems and discuss their respective advantages and applications. Also, we dissect the translational components required for ncAA incorporation and compile lists of ncAAs that can be incorporated into polypeptides via different acylation approaches. We highlight the recent progress in using unnatural nucleobase pairs to increase the repertoire of orthogonal codons, as well as using tRNA-specific ribozymes for in situ acylation. We summarize advances in engineering of translational machinery such as tRNAs, aminoacyl-tRNA synthetases, elongation factors, and ribosomes to achieve efficient incorporation of structurally challenging ncAAs. We note that, many engineered components of biosynthetic machinery are developed for the use in vivo but are equally applicable to the in vitro systems. These are included in the review to provide a comprehensive overview for ncAA incorporation and offer new insights for the future development in cell-free systems. Finally, we highlight the exciting progress in the genomic engineering, resulting in E. coli strains free of amber and some redundant sense codons. These strains can be used for preparation of cell extracts offering multiple reassignment options.

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Clay Mineral Minerals as a Strategy for Biomolecule Incorporation: Amino Acids Approach.

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