A modular approach to enzymatic ligation of peptides and proteins with oligonucleotides

Tan, D.; Cheong, Vee Vee; Lim, Kah Wai; Phan, Anh Tuân

doi:10.1039/d1cc01348c

Cited by 4 publications

(4 citation statements)

References 41 publications

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“…Various DNA origami architectures including squares, [23,24] triangles, [25][26][27] disks, [28] cubes, [29] boxes, [30,31] wireframes [32] have been made since Rothemund first reported DNA origami [33] . Benefiting from sequential specificity and spatial addressability, DNA origami offers an ideal platform to attach proteins at predefined sites via a set of immobilization strategies such as non-specific electrostatic adsorption, [34] site-specific assembly of DNA modified protein, [35] or direct assembly assisted by protein tags, [36] aptamers, [37] antibody-antigen binding, [38] and enzymatic ligation, [39] showing fantastic designability and accuracy for protein manipulation.…”

Section: Dna Origami Structure Classificationmentioning

confidence: 99%

DNA Origami‐Based Protein Manipulation Systems: From Function Regulation to Biological Application

Huang

Yin

et al. 2022

ChemBioChem

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Proteins directly participate in tremendous physiological processes and mediate a variety of cellular functions. However, precise manipulation of proteins with predefined relative position and stoichiometry for understanding protein‐protein interactions and guiding cellular behaviors is still challenging. With superior programmability of DNA molecules, DNA origami technology is able to construct arbitrary nanostructures that can accurately control the arrangement of proteins with various functionalities to solve these problems. Herein, starting from the classification of DNA origami nanostructures and the category of assembled proteins, we summarize the existing DNA origami‐based protein manipulation systems (PMSs), review the advances on the regulation of their functions, and discuss their applications in cellular behavior modulation and disease therapy. Moreover, the limitations and potential directions of DNA origami‐based PMSs are also presented, which may offer guidance for rational construction and ingenious application.

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Section: Dna Origami Structure Classificationmentioning

confidence: 99%

DNA Origami‐Based Protein Manipulation Systems: From Function Regulation to Biological Application

Huang

Yin

et al. 2022

ChemBioChem

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“…Based on the proteins database, the localization of REJ in different exons separated by many introns led us to clone the REJ gene via the phosphoramidite synthetic method. Therefore, we designed REJ nucleotide sequences and sent them to Synbio, US, to create a product that was identical to the product that was theoretically proposed [25]. Similarly, Schröder et al, 2011, studied the segments of small molecular weight of an expressed REJ protein.…”

Section: Rej-his Fusion Protein Expressionmentioning

confidence: 99%

Cloning and Expression of Receptor of Egg Jelly Protein of Polycystic Kidney Disease 1 Gene in Human Receptor of Egg Jelly Protein

Sonbol¹,

AlRashidi²

2022

Pharmacophore

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Autosomal dominant polycystic kidney disease (ADPKD) is caused by a mutation in the polycystic kidney disease1 (PKD1) gene, which is responsible for 85% of ADPKD cases. The PKD1 gene encodes a polycystin-1 (PC1) protein that has a large extracellular area containing many polypeptide motifs. The extracellular region of PC1 includes several well-defined peptide domains that show that it has been involved in cell-cell and/or cell-matrix interactions. One of the regions that we focused on in this study is the receptor of the egg jelly (REJ) domain. This study conveys novel findings, in which we utilized a successful methodology to clone and express the REJ protein. The REJ gene is located in many exons separated by introns, which made it impossible to clone the whole REJ region. Therefore, synthetic DNA technology was used to clone a fragment located on exon 15 of the REJ gene. The PCR technology was used to amplify the REJ region by using a universal primer to express the domain located on exon 15 in humans. The REJ from synthetic DNA was cloned by using the phosphoramidite synthetic method. Sequencing technology and bioinformatic tools were applied to confirm the validation of the coding region. The results indicated that we successfully cloned and expressed the REJ protein using the DNA synthesis method instead of the conventional methodology.This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial-Share Alike 4.0 License, which allows others to remix, tweak, and build upon the work non commercially, as long as the author is credited and the new creations are licensed under the identical terms.

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“…In contrast, Met, Val, Leu, and Ile containing hydrophobic but larger side chain have the tendency to significantly reduce ligase activity. As a result, this enhanced mutant, also known as OaAEP1b C247A, has been widely used as a valuable tool for the modifications and labelling of proteins and peptides [92][93][94][95][96][97] . Additionally, three new ligases namely OaAEP3-5 from O. affinis were discovered and characterized 98 .…”

Section: Oaaep1b and Its Mutant Variantsmentioning

confidence: 99%

Expanding the scope of substrate specificity for peptide asparaginyl ligases

Lim¹

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A modular approach to enzymatic ligation of peptides and proteins with oligonucleotides

Abstract: A modular approach has been developed for enzymatic ligation of peptides/proteins with oligonucleotides through the design of tag phosphoramidites as adaptors, paving the way towards streamlined production of peptide/protein-oligonucleotide conjugates.

Cited by 4 publications

References 41 publications

DNA Origami‐Based Protein Manipulation Systems: From Function Regulation to Biological Application

DNA Origami‐Based Protein Manipulation Systems: From Function Regulation to Biological Application

Cloning and Expression of Receptor of Egg Jelly Protein of Polycystic Kidney Disease 1 Gene in Human Receptor of Egg Jelly Protein

Expanding the scope of substrate specificity for peptide asparaginyl ligases

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