Protein Assembly by Orthogonal Chemical Ligation Methods

Nilsson, Bradley L.; Hondal, Robert J.; Soellner, Matthew B.; Raines, Ronald T.

doi:10.1021/ja029752e

Cited by 144 publications

(104 citation statements)

References 18 publications

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“…[15,16] In an impressive effort demonstrating the power of methods involving orthogonal chemical ligation, Raines and co-workers completed the total synthesis of ribonuclease A (31, RNAse A, 124 amino acids) by linking three fragments (Scheme 7). [17] RNAse A(110-111) was synthesized as the Cterminal phosphanyl thioester FmocCys(Trt)Glu(OtBu)- …”

Section: Peptide Ligationmentioning

confidence: 99%

The Staudinger Ligation—A Gift to Chemical Biology

2004

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Although the reaction between an azide and a phosphane to form an aza-ylide was discovered by Hermann Staudinger more than 80 years ago and has found widespread application in organic synthesis, its potential as a highly chemoselective ligation method for the preparation of bioconjugates has been recognized only recently. As the two reaction partners are bioorthogonal to almost all functionalities that exist in biological systems and react at room temperature in an aqueous environment, the Staudinger ligation has even found application in the complex environment of living cells. Herein we describe the current state of knowledge on this reaction and its application both for the preparation of bioconjugates and as a ligation method in chemical biology.

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Section: Peptide Ligationmentioning

confidence: 99%

The Staudinger Ligation—A Gift to Chemical Biology

2004

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“…[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16] High chemoselectivity, stability, and compatibility with protic solvents, and even aqueous media, are requirements for such ligations.…”

Section: Introductionmentioning

confidence: 99%

Dechalcogenative Allylic Selenosulfide and Disulfide Rearrangements: Complementary Methods for the Formation of Allylic Sulfides in the Absence of Electrophiles. Scope, Limitations, and Application to the Functionalization of Unprotected Peptides in Aqueous Media.

et al. 2007

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Primary allylic selenosulfates (seleno Bunte salts) and selenocyanates transfer the allylic selenide moiety to thiols giving primary allylic selenosulfides, which undergo rearrangement in the presence of PPh 3 with the loss of selenium to give allylically rearranged allyl alkyl sulfides. This rearrangement may be conducted with prenyl-type selenosulfides to give isoprenyl alkyl sulfides. Alkyl secondary and tertiary allylic disulfides, formed by sulfide transfer from allylic heteroaryl disulfides to thiols, undergo desulfurative allylic rearrangement on treatment with PPh 3 in methanolic acetonitrile at room temperature. With nerolidyl alkyl disulfides this rearrangement provides an electrophile-free method for the introduction of the farnesyl chain onto thiols. Both rearrangements are compatible with the full range of functionality found in the proteinogenic amino acids and it is demonstrated that the desulfurative rearrangement functions in aqueous media, enabling the derivatization of unprotected peptides. It is also demonstrated that the allylic disulfide rearrangement can be inducted in the absence of phosphine at room temperature by treatment with piperidine, or simply by refluxing in methanol. Under these latter conditions the reaction is also applicable to allyl aryl disulfides, providing allylically rearranged allyl aryl sulfides in good yields.

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“…20 The initial intermediate is an iminophosphorane that rearranges to an amido phosphonium salt which hydrolyses to the amide (Scheme 8). Azides are involved in the synthesis of proteins by native chemical ligation (NCL), the method of choice for the preparation of large peptides and proteins (see later).…”

Section: Azidesmentioning

confidence: 99%

Evolution of amide bond formation

Joullié¹,

Lassen²

2010

Arkivoc

160

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This paper is dedicated to Drs Bruce E. Maryanoff and Cynthia A. Maryanoff for their outstanding contribution to organic chemistry as industrial chemists AbstractThe presence of carboxamide groups is found in a large array of biologically important compounds. Peptides and proteins play an important role in modern biology. A key step in peptide production is the formation of the peptide bond, which involves amide bond formation. Chemical synthesis of large peptides by intermolecular coupling of smaller peptides using conventional peptide bond-forming techniques did not realize its potential advantages until recently. Using an approach based on highly specific and efficient chemical ligation of two peptide segments, the two subunits were ligated to form a new peptide bond. Native chemical ligation extended the concept by creating a native peptide bond and providing new approaches to protein engineering.

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Protein Assembly by Orthogonal Chemical Ligation Methods

Cited by 144 publications

References 18 publications

The Staudinger Ligation—A Gift to Chemical Biology

The Staudinger Ligation—A Gift to Chemical Biology

Dechalcogenative Allylic Selenosulfide and Disulfide Rearrangements: Complementary Methods for the Formation of Allylic Sulfides in the Absence of Electrophiles. Scope, Limitations, and Application to the Functionalization of Unprotected Peptides in Aqueous Media.

Evolution of amide bond formation

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