In search of new methods in peptide synthesis. A review of the last three decades

Bodanszky, Miklos

doi:10.1111/j.1399-3011.1985.tb02200.x

Cited by 35 publications

(4 citation statements)

References 124 publications

(3 reference statements)

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“…A coupling reagent needs to be able to cope with this whole portfolio of reactivity. Many reviews on coupling reagents have been published, [8][9][10][11][12][13][14] illustrating their importance in the synthetic armoury of the synthetic chemist, but these reviews have often failed to offer a critical view on the subject making the choice of reagent difficult. An important issue is that many of the coupling reagents reported have not been compared to others, making any real evaluation impossible.…”

Section: Introductionmentioning

confidence: 99%

Amide bond formation: beyond the myth of coupling reagents

2009

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Amide bond formation is a fundamentally important reaction in organic synthesis, and is typically mediated by one of a myriad of so-called coupling reagents. This critical review is focussed on the most recently developed coupling reagents with particular attention paid to the pros and cons of the plethora of "acronym" based reagents. It aims to demystify the process allowing the chemist to make a sensible and educated choice when carrying out an amide coupling reaction (179 references).

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Section: Introductionmentioning

confidence: 99%

Amide bond formation: beyond the myth of coupling reagents

2009

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“…Peptides can be synthesized chemically via stepwise addition of amino acid (AA) monomers. − The conventional chemical synthesis route consists of solid phase peptide synthesis (SPPS) , and liquid phase peptide synthesis (LPPS) (Figure ). Membrane enhanced peptide synthesis (MEPS) improves the LPPS route by replacing extraction, precipitation, microfiltration, and drying with diafiltration , − and has the advantage of a significantly shorter processing time. , Previous studies have shown that this iterative approach can achieve high yield and purity for peptide, oligonucleotide, and monodisperse polyethylene glycol (PEG). − …”

Section: Introductionmentioning

confidence: 99%

Implication of Side Reactions in Iterative Biopolymer Synthesis: The Case of Membrane Enhanced Peptide Synthesis

Chen

Sharifzadeh

Shah

et al. 2017

Ind. Eng. Chem. Res.

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Membrane enhanced peptide synthesis (MEPS) improves conventional liquid phase synthesis by purifying intermediate products via filtration. A challenging aspect of MEPS is the propagation of unreacted materials and by-products throughout the iterative synthesis. In this study, we first develop and validate a model of MEPS. The model is then applied to investigate the implications of sidereactions (i.e. formation of error sequences) due to incomplete reaction and insufficient removal of amino acids after coupling. Sensitivity analysis shows that increasing the reaction extent for all couplings from 90% to 100% reduces the yield of truncated sequences from 29% to 0%. The formation of repeating sequences is found to be negligible in all case studies due to the large diavolume of postdeprotection diafiltration. This study provides useful insights into the operation of MEPS with particular emphasis on the control of error sequence formation. These insights are transferable to other sequencecontrolled biopolymer syntheses.

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“…Despite this high variability, the chemical synthesis of peptides can be easily implemented with great rapidity and high production rates. This aspect is of particular interest, as the availability of well-grounded and straightforward synthetic protocols allows several sequences to be tested in a short time, thus making these biomolecules highly competitive in pharmaceutical, as well as sensing, applications [20]. Therefore, genetically encoded peptide ligands with tailored properties can be generated by screening large combinatorial libraries using in-vitro display techniques [21].…”

Section: Peptide Selection Synthesis and Characterisationmentioning

confidence: 99%

The Role of Peptides in the Design of Electrochemical Biosensors for Clinical Diagnostics

et al. 2021

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Peptides represent a promising class of biorecognition elements that can be coupled to electrochemical transducers. The benefits lie mainly in their stability and selectivity toward a target analyte. Furthermore, they can be synthesized rather easily and modified with specific functional groups, thus making them suitable for the development of novel architectures for biosensing platforms, as well as alternative labelling tools. Peptides have also been proposed as antibiofouling agents. Indeed, biofouling caused by the accumulation of biomolecules on electrode surfaces is one of the major issues and challenges to be addressed in the practical application of electrochemical biosensors. In this review, we summarise trends from the last three years in the design and development of electrochemical biosensors using synthetic peptides. The different roles of peptides in the design of electrochemical biosensors are described. The main procedures of selection and synthesis are discussed. Selected applications in clinical diagnostics are also described.

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In search of new methods in peptide synthesis. A review of the last three decades

Cited by 35 publications

References 124 publications

Amide bond formation: beyond the myth of coupling reagents

Amide bond formation: beyond the myth of coupling reagents

Implication of Side Reactions in Iterative Biopolymer Synthesis: The Case of Membrane Enhanced Peptide Synthesis

The Role of Peptides in the Design of Electrochemical Biosensors for Clinical Diagnostics

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