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Analiza związków lotnych z wykorzystaniem bioczujników na bazie syntetycznych peptydów

Wasilewski Tomasz

Analityka : nauka i praktyka

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2021

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nr 4

24--29

PL

Artykuł powstał na podstawie rozprawy doktorskiej pt.: 'Syntetyczne peptydy jako materiały do budowy czujników' nagrodzonej przez Komitet Chemii Analitycznej PAN w 2021 roku w konkursie na najlepsze prace doktorskie, nagroda ufundowana przez firmę LGC Standards.

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Metody chemicznej ligacji w syntezie peptydów i białek. Część 2

Jędrzejewska K., Kropidłowska M., Wieczerzak E.

Wiadomości Chemiczne

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2017

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[Z] 71, 9-10

747--761

EN

Proteins are synthesized only by living organisms. Today, we are able to receive them by recombinant protein expression in bacterial cells. This technique is very useful and gives satisfactory amount of desirable material but it precludes the possibility of introduction of some chemical modifications that are often obligatory. For this reason, chemical synthesis of longer peptide chains is still important and is the object of scientists attention. Over the last century, notion of peptide synthesis took a new meaning. Nowadays, we know a number of innovative methods and also automated devices which help us to make progress in this area. Nevertheless, the synthesis of longer, more complicated peptide chains and proteins still constitutes a problem. Native chemical ligation (NCL) has facilitated the synthesis of numerous complex peptide and protein targets. Expansion of ligation techniques has allowed the entry of peptides into the world of therapeutic drugs [1]. NCL reactions are carried out in aqueous solution and give good yields. Due to mild conditions, NCL overcomes racemic and solubility problems encountered in classical peptide synthesis using protected fragments. The challenge is to synthesize the C-terminal thioester-containing peptide necessary for the transesterification reaction, which is the first step of linking the peptide fragments [2]. In this review we discuss the evolution, advantages and potential applications of chemical ligation reactions. In the first part of this article we described the utility of native chemical ligation approach to non-cysteine containing peptides. This part details a number of important approaches to the synthesis of peptides bearing a C-terminal thioester. Contemporary applications of these techniques to the total chemical synthesis of proteins are also presented.

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Metody chemicznej ligacji w syntezie peptydów i białek. Część 1

Kropidłowska M., Jędrzejewska K., Wieczerzak E.

Wiadomości Chemiczne

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2017

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[Z] 71, 9-10

727--746

EN

Proteins are biological macromolecules affecting very important functions in the body. They are involved in many biochemical processes. They can perform catalytic functions acting as enzymes. They also participate in the transport of many small molecules and ions – for example one molecule of hemoglobin carries four molecules of oxygen. In addition, proteins serve as antibodies and are involved in transmission of nerve impulses as receptor proteins. Because peptides and proteins perform so important functions, to study them it is essential to obtain these compounds in the greatest possible amounts. The compounds can be obtained generally by three main methods: • by isolation of the native peptides and proteins • by expression in microorganisms • by chemical synthesis. Each of the above methods has its advantages and disadvantages, but only the chemical synthesis gives the possibility to introduce modifications to the structure of the resulting protein, such as the insertion of new functional groups, to give the product in the final form and with satisfactory yield. In this review we present the application of chemical ligation methods in the synthesis of peptides and proteins. We describe in details mechanism of native chemical ligation method and the conditions necessary to carry the reaction [1]. The synthesis of long polypeptide chains by kinetically controlled ligation (KCL) is also depicted [2]. This part of the paper also details a number of approaches to noncysteine containing peptides by chemical ligation methods.

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Synthesis of Endothiopeptides by Using the 'Azirine/Oxazolone Method'

Bärtsch A., Bischof B., Heimgartner H.

Polish Journal of Chemistry

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2009

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Vol. 83, nr 2

195-206

EN

The reaction of tert-butyl- or THP-pro tected mandelic thioacid (7a and 7b) with N,N,2,2-tetramethyl-2H-azirin-3-amine (2a) gave the dipeptide analogues tBu- and THP-Mns-Aiby[CS]NMe2 (8a and 8b, resp.) with a C-terminal thioamide group. Treatment of 8a with HCl gas in toluene led to 2-(1-tert-butoxy benzyl)-4,4- dimethyl-1,3-thiazole-5(4H)-one (9), which reacted with dimethylamine via ring opening to give tBu-Mnsy[CSNH]Aib-NMe2 (11a), an isomer of 8a with the thioamide group within the chain, i.e., the product of a sulfur migration. In the case of 8b, selective deprotection of the THP-hydroxy group was achieved by treatment with pyridinium p-toluenesulfonate (PPTS) in ethanol. Cyclization of the resulting Mns-Aiby[CS]NMe2 (13) yielded the 2-thioxomorpholin-5-one 10. In a similar manner, Boc-Val-SH (14) reacted with azirine 2b to give Boc-Val-Aiby[CS]N(Me)Ph (15a), which was transformed to Fmoc-Val-Aiby[CS]N(Me)Ph (15b) and further to Fmoc-Valy[CSNH]Aib-N(Me)Ph (16) by treatment with ZnCl2 in acetic acid. Coupling of two of these molecules via the 1,3-thiazol-5(4H)-one 17 yielded the endodithiopeptide Fmoc- Valy[CSNH]Aib-Valy[CSNH]Aib-N(Me)Ph (19).

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Terpenic Alcohols - Source of Chirality in Condensing Reagents in Peptide Chemistry

Kamiński Z., Kolesińska B., Markowicz S., Pokrzeptowicz K.

Polish Journal of Chemistry

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1999

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Vol. 73, nr 12

1965-1968

EN

Chiral 2,4-dichloro-6-terpenyloxy-1,3,5-triazines 3a-d obtained by treatment of cyanuric chloride with isomyrtanol (1), nopol (2), isopinocampheol (3) and borneol (4) are useful as enantiodifferentiating coupling reagent in the synthesis of dipeptides

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Proinsulin C-peptides from bovine, ovine and bisontine pancreata

Izdebski J., Fiertek D., Majewski T.

Polish Journal of Chemistry

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1998

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Vol. 72, nr 3

548-553

EN

Two C-peptides corresponding to sequences of genetic variants of bovine proinsulin have been synthesized by solid-phase method. C-peptide containing material has been isolated from two bovine pancreata using acid-ethanol extraction, gel filtration on Sephadex G-50 and ion exchange chromatography on carboxymethyl cellulose. Comparison of these materials with synthetic standards on reverse-phase HPLC have revealed that both pancreata contained only one variant of C-peptide which had Pro in position 16. The second variant of bovine proinsulin C-peptide with Leu at this position has not been detected. The corresponding genetic variant of bovine proinsulin, containing Leu within C-peptide sequence, has been found by other authors in the material obtained from a pool of large number of pancreata. Our results exclude the possibility that the two bovine proinsulins are a result of expression of two insulin genes in the bovine species as a whole. The same C-peptide was found in ovine and bisontine pancreata.