Eine neue Umlagerungsreaktion und ein neues Prinzip zum Aufbau von Peptidketten

Brenner, M.; Zimmermann, J.; Wehrmüller, J.; Quitt, P.; Photaki, Iphigenia

doi:10.1007/bf02158504

Cited by 45 publications

(11 citation statements)

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“…It consisted of preparation of corticotrophin selectively acetylated on its terminal serine. 633 Although being possible only under highly denaturing conditions of alkali exposure, the approach allowed for a spontaneous intramolecular O -N acyl transfer 634 on the N-terminal Ser residues, while O-acetyl groups of in-chain Ser, Thr and Tyr residues were hydrolysed. The general idea of overcoming the entropy barrier of an otherwise slow intermolecular process by bringing two reacting partners together through a covalent linkage to initialize an intramolecular reaction has been later transformed into a large variety of selective modification reactions.…”

Section: Serine and Threoninementioning

confidence: 99%

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

2015

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Bioconjugation methodologies have proven to play a central enabling role in the recent development of biotherapeutics and chemical biology approaches. Recent endeavours in these fields shed light on unprecedented chemical challenges to attain bioselectivity, biocompatibility, and biostability required by modern applications. In this review the current developments in various techniques of selective bond forming reactions of proteins and peptides were highlighted. The utility of each endogenous amino acid-selective conjugation methodology in the fields of biology and protein science has been surveyed with emphasis on the most relevant among reported transformations; selectivity and practical use have been discussed.

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Section: Serine and Threoninementioning

confidence: 99%

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

2015

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“…Regarding the spontaneous X → N acyl migration, Wieland showed in the early 1950s that Saminoacyl-cysteine derivatives undergo an intramolecular transacylation to form N α -aminoacyl-cysteine compounds as shown in Scheme 6 [151]. The concept of entropic activation, and its significance in the context of peptide bond formation via intramolecular acyl transfer, was introduced by Brenner [152,153] and then further developed by Kemp to the Prior Thiol Capture Strategy [154]. This principle was subsequently applied almost simultaneously by Kent [155] and Tam [156] for the development of a highly chemoselective ligation of unprotected peptide fragments via peptide amide bonds to produce larger polypeptide chains and proteins.…”

Section: Cysteine As Nucleophile In Proteinsmentioning

confidence: 99%

Isosteric replacement of sulfur with other chalcogens in peptides and proteins

2005

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The review addresses the functional and structural properties of the two series of chalcogen analogues of amino acids in peptides and proteins, the methionine and the serine/cysteine series, and discusses the synthesis of the related selenium/tellurium analogues as well as their use in peptide synthesis and protein expression. Advances in synthetic methodologies and recombinant technologies and their combined applications in native and expressed protein ligation allows the isomorphous character of selenium- and tellurium-containing amino acids to be exploited for production of heavy metal mutants of proteins and thus to facilitate the phasing problem in x-ray crystallography. In addition, selenocysteine has been recognized as an ideal tool for the production of selenoenzymes with new catalytic activities. Moreover, the fully isomorphous character of disulfide replacement with diselenide is well suited to increase the robustness of cystine frameworks in cystine-rich peptides and proteins and for the de novo design of even non-native cystine frameworks by exploiting the highly negative redox potential of selenols.

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“…Chemoselective ligation, often based on thiol and imine chemistries, employs a pair of mutually reactive nucleophile and electrophiles to couple two unprotected peptide segments, usually as a nonamide linkage as surrogate bonds at ligation sites 37. Examples include hydrazone,38–40 oxime,41 thioether,42, 43 and thioester 44–48. An advantage of these peptide‐bond replacement methods is the greater efficiency of ligation reaction deriving from the high and specific reactivity between the two functional groups that is often not seen in amino acids.…”

Section: Conceptual Framework Of Orthogonal Ligationmentioning

confidence: 99%

Orthogonal ligation strategies for peptide and protein

1999

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This review focuses on the concept, criteria, and methods of an orthogonal amide ligating strategy suitable for syntheses of peptides, peptide mimetics, and proteins. Utilizing unprotected peptides or proteins derived from chemical or biosynthetic sources, this ligation strategy has been shown to be general and exceptionally mild. Its orthogonality in ligating two unprotected segments with free N‐terminal (NT)‐amines at a specific NT‐amine is achieved through a chemoselective capture step and then an intramolecular acyl transfer reaction. Both coupling reagents for enthalpic activation and protection schemes therefore become unnecessary. More than a dozen orthogonal ligation methods based on either imine or thioester captures have been developed to afford native and unusual amino acids at ligation sites of linear, branched, or cyclic peptides. Because unprotected peptides and proteins of different sizes and forms can be obtained from either chemical or recombinant sources, orthogonal ligation removes the size limitation imposed on the chemical synthesis of a protein with a native or non‐native structure. Furthermore, by using building blocks from biosynthetic sources, orthogonal ligation provides a unifying operational concept for both total and semisynthesis of peptides and proteins. © 2000 John Wiley & Sons, Inc. Biopoly 51: 311–332, 1999

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Eine neue Umlagerungsreaktion und ein neues Prinzip zum Aufbau von Peptidketten

Cited by 45 publications

References 1 publication

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

Isosteric replacement of sulfur with other chalcogens in peptides and proteins

Orthogonal ligation strategies for peptide and protein

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