scholarly journals Flow-based Methods in Chemical Peptide and Protein Synthesis

2021 ◽  
Vol 75 (6) ◽  
pp. 480-483
Author(s):  
Kevin Schiefelbein ◽  
Nina Hartrampf

Flow chemistry has emerged as a powerful method for on-demand chemical synthesis and modification of peptides and proteins. Herein, we discuss the characteristics of flow chemistry and how they are applied to various aspects of peptide chemistry. We highlight recent advances in automated flow-based peptide synthesis, which extend the length of peptides routinely accessible to single-domain proteins and allow for the collection of time-resolved synthesis data. Applications of this data for the prediction of synthesis outcome and the potential for the development of more sustainable synthesis methods are also discussed. Finally, we will review solutionphase approaches, including flow-based ligation strategies and peptide cyclization. Throughout this review, the current challenges and potential future developments are highlighted.

2015 ◽  
Vol 3 (1) ◽  
pp. 107-116 ◽  
Author(s):  
Yi-Chao Huang ◽  
Ge-Min Fang ◽  
Lei Liu

Abstract Protein chemical synthesis offers useful and otherwise-difficulty-to-obtain biomacromolecules for biological and pharmaceutical studies. Recently, the hydrazide chemistry has drawn attentions in this field as peptide or protein hydrazides can be used as key intermediates for different synthesis and modification purposes. Besides being a traditional bioorthogonal chemical handle, a hydrazide group can serve as a readily accessible precursor of a thioester. This strategy significantly improves the efficiency and scope of native chemical ligation for protein chemical synthesis. Here we review the chemical transformations of peptide or protein hydrazides and total/semi/enzymatic protein synthesis methods involving peptide or protein hydrazides. Several examples of protein chemical synthesis using peptide hydrazides as key intermediates are described.


2013 ◽  
Vol 2 (3) ◽  
Author(s):  
Ian R. Baxendale ◽  
Laurens Brocken ◽  
Carl J. Mallia

2018 ◽  
Vol 7 (3) ◽  
pp. 875-884 ◽  
Author(s):  
Ana I. Benítez-Mateos ◽  
Irantzu Llarena ◽  
Ana Sánchez-Iglesias ◽  
Fernando López-Gallego

Catalysts ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 663
Author(s):  
Christophe Len ◽  
Renzo Luisi

Continuous flow chemistry is radically changing the way of performing chemical synthesis, and several chemical and pharmaceutical companies are now investing in this enabling technology [...]


2019 ◽  
Vol 2019 ◽  
pp. 1-15 ◽  
Author(s):  
Merly de Armas-Ricard ◽  
Enrique Ruiz-Reyes ◽  
Oney Ramírez-Rodríguez

Polyphenols are secondary metabolites of plants and include a variety of chemical structures, from simple molecules such as phenolic acids to condensed tannins and highly polymerized compounds. Caffeic acid (3,4-dihydroxycinnamic acid) is one of the hydroxycinnamate metabolites more widely distributed in plant tissues. It is present in many food sources, including coffee drinks, blueberries, apples, and cider, and also in several medications of popular use, mainly those based on propolis. Its derivatives are also known to possess anti-inflammatory, antioxidant, antitumor, and antibacterial activities, and can contribute to the prevention of atherosclerosis and other cardiovascular diseases. This review is an overview of the available information about the chemical synthesis and antioxidant activity of caffeic acid derivatives. Considering the relevance of these compounds in human health, many of them have been the focus of reviews, taking as a center their obtaining from the plants. There are few revisions that compile the chemical synthesis methods, in this way, we consider that this review does an important contribution.


Science ◽  
2020 ◽  
Vol 368 (6494) ◽  
pp. 980-987 ◽  
Author(s):  
N. Hartrampf ◽  
A. Saebi ◽  
M. Poskus ◽  
Z. P. Gates ◽  
A. J. Callahan ◽  
...  

Ribosomes can produce proteins in minutes and are largely constrained to proteinogenic amino acids. Here, we report highly efficient chemistry matched with an automated fast-flow instrument for the direct manufacturing of peptide chains up to 164 amino acids long over 327 consecutive reactions. The machine is rapid: Peptide chain elongation is complete in hours. We demonstrate the utility of this approach by the chemical synthesis of nine different protein chains that represent enzymes, structural units, and regulatory factors. After purification and folding, the synthetic materials display biophysical and enzymatic properties comparable to the biologically expressed proteins. High-fidelity automated flow chemistry is an alternative for producing single-domain proteins without the ribosome.


2005 ◽  
Vol 288 (5) ◽  
pp. E1028-E1037 ◽  
Author(s):  
Britt-Marie Iresjö ◽  
Elisabeth Svanberg ◽  
Kent Lundholm

Murine L6 and human rhabdomyosarcoma cells were cultured standardized in low (0.28 mM) and normal (9 mM) amino acid (AA) concentrations to reevaluate by independent methods to what extent AA activate initiation of protein synthesis. Methods used were incorporation of radioactive AA into proteins, distribution analysis of RNA in density gradient, and Western blots on initiation factors of translation of proteins in cultured cells as well as in vivo (gastrocnemius, C57Bl mice) during starvation/refeeding. Incorporation rate of AA gave incorrect results in a variety of conditions, where phenylalanine stimulated the incorporation rate of phenylalanine into proteins, but not of tyrosine, and tyrosine stimulated incorporation of tyrosine but not of phenylalanine. Similar problems were observed when [35S]methionine was used for labeling of fractionated cellular proteins. However, the methods entirely independent of labeled AA incorporation indicated that essential AA activate initiation of translation, whereas nonessential AA did not. Branched-chain AA and glutamine, in combination with some other AA, also stimulated initiation of translation. Starvation/refeeding in vitro agreed qualitatively with results in vivo evaluated by initiation factors. Insulin at physiological concentrations (100 μM/ml) did not stimulate global protein synthesis at low or normal AA concentrations but did so at supraphysiological levels (3 mU/ml), confirmed by independent methods. Our results reemphasize that labeled AA should be used with caution for quantification of protein synthesis, since the precursor pool(s) for protein synthesis is not in complete equilibrium with surrounding AA. “Flooding” tracee experiments did not overcome this problem.


2012 ◽  
Vol 622-623 ◽  
pp. 556-560
Author(s):  
Gholamreza Kiani ◽  
Mojtaba Shahi ◽  
Ali Rostami

Novel combined electrochemical and chemical synthesis methods for the preparation of Polypyrrole-based actuators are presented. Polypyrrole (PPy) actuators were electrochemically synthesized and after coating with a thin gold nano-layer, prepared into a Polyethersulfone (PI) substrate. Scanning Tunneling Microscopy (STM) and a potentiostat–galvanostat were used to confirm the actuation of PPy based actuators during the redox process. Three-layer actuator based on polypyrrole as electroactive material, Polyethersulfone as substrate and gold nanolayer in our proposed method have been realized. The structure strength and layer adhesion have been improved. This advancement in conducting polymer actuator technology will impact many engineering fields, where a stable, lightweight and large displacement actuator is needed.


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