Metal-free approach for hindered amide-bond formation with hypervalent iodine(iii) reagents: application to hindered peptide synthesis

2021 ◽  
Author(s):  
Hyo-Jun Lee ◽  
Xiao Huang ◽  
Shigeyoshi Sakaki ◽  
Keiji Maruoka
Keyword(s):  
Peptide Synthesis ◽  
Hydrogen Fluoride ◽  
Bond Formation ◽  
Amide Bond ◽  
Hypervalent Iodine ◽  
Fluoride Complex ◽  
Metal Free ◽  
Amino Esters ◽  
Amide Bond Formation

A new, bulky amide and peptide synthesis with hypervalent iodine(iii) reagent/pyridine–hydrogen fluoride complex under mild and metal-free conditions was developed by using α-amino esters with potential activating group (PAG) at the ester residue.

Non-Classical Amide Bond Formation: Transamidation and Amidation of Activated Amides and Esters by Selective N–C/O–C Cleavage

Synthesis ◽  
2020 ◽  
Vol 52 (18) ◽  
pp. 2579-2599 ◽  
Author(s):  
Michal Szostak ◽  
Guangchen Li
Keyword(s):  
Transition Metal ◽  
Bond Activation ◽  
Bond Formation ◽  
Amide Bond ◽  
Acyl Transfer ◽  
Metal Free ◽  
Amide Bond Formation ◽  
New Methods ◽  
Formidable Challenge ◽  
Tetrahedral Intermediates

In the past several years, tremendous advances have been made in non-classical routes for amide bond formation that involve transamidation and amidation reactions of activated amides and esters. These new methods enable the formation of extremely valuable amide bonds via transition-metal-catalyzed, transition-metal-free, or metal-free pathways by exploiting chemoselective acyl C–X (X = N, O) cleavage under mild conditions. In a broadest sense, these reactions overcome the formidable challenge of activating C–N/C–O bonds of amides or esters by rationally tackling nN → π*C=O delocalization in amides and nO → π*C=O donation in esters. In this account, we summarize the recent remarkable advances in the development of new methods for the synthesis of amides with a focus on (1) transition-metal/NHC-catalyzed C–N/C–O bond activation, (2) transition-metal-free highly selective cleavage of C–N/C–O bonds, (3) the development of new acyl-transfer reagents, and (4) other emerging methods.1 Introduction2 Transamidation of Amides2.1 Transamidation by Metal–NHC Catalysis (Pd–NHC, Ni–NHC)2.2 Transition-Metal-Free Transamidation via Tetrahedral Intermediates2.3 Reductive Transamidation2.4 New Acyl-Transfer Reagents2.5 Tandem Transamidations3 Amidation of Esters3.1 Amidation of Esters by Metal–NHC Catalysis (Pd–NHC, Ni–NHC)3.2 Transition-Metal-Free Amidation of Esters via Tetrahedral Intermediates3.3 Reductive Amidation of Esters4 Transamidations of Amides by Other Mechanisms5 Conclusions and Outlook

Substrate-Controlled Amide Bond Formation: Innovation of Peptide Synthesis

2021 ◽  
Vol 79 (5) ◽  
pp. 382-390
Author(s):  
Tomohiro Hattori ◽  
Wataru Muramatsu ◽  
Hisashi Yamamoto
Keyword(s):  
Peptide Synthesis ◽  
Bond Formation ◽  
Amide Bond ◽  
Amide Bond Formation

A new reagent for the mediation of amide bond formation in peptide synthesis.

1984 ◽  
Vol 25 (42) ◽  
pp. 4825-4828 ◽  
Author(s):  
Robert Ramage ◽  
Christopher P. Ashton ◽  
David Hopton ◽  
Maxwell J. Parrott
Keyword(s):  
Peptide Synthesis ◽  
Bond Formation ◽  
Amide Bond ◽  
Amide Bond Formation

3,6-Di(pyridin-2-yl)-1,2,4,5-tetrazine (pytz) catalysed metal-free amide bond formation from thioacids and amines at room temperature

2020 ◽  
Vol 61 (35) ◽  
pp. 152272
Author(s):  
Suvendu Samanta ◽  
Shounak Ray ◽  
Samanka Narayan Bhaduri ◽  
Partha Kumar Samanta ◽  
Papu Biswas
Keyword(s):  
Room Temperature ◽  
Bond Formation ◽  
Amide Bond ◽  
Metal Free ◽  
Amide Bond Formation

scholarly journals Real-time monitoring of solid-phase peptide synthesis using a variable bed flow reactor

2019 ◽  
Vol 55 (97) ◽  
pp. 14598-14601 ◽  
Author(s):  
Eric T. Sletten ◽  
Manuel Nuño ◽  
Duncan Guthrie ◽  
Peter H. Seeberger
Keyword(s):  
Real Time ◽  
Peptide Synthesis ◽  
Flow Reactor ◽  
Solid Phase ◽  
Bond Formation ◽  
Solid Phase Peptide Synthesis ◽  
Amide Bond ◽  
Real Time Monitoring ◽  
Amide Bond Formation

Integration of a pressure-based variable bed flow reactor into an automated solid-phase peptide synthesizer allowed for monitoring of on-resin aggregation and incomplete amide bond formation in real-time.

scholarly journals Structural and mutational analysis of the nonribosomal peptide synthetase heterocyclization domain provides insight into catalysis

2016 ◽  
Vol 114 (1) ◽  
pp. 95-100 ◽  
Author(s):  
Kristjan Bloudoff ◽  
Christopher D. Fage ◽  
Mohamed A. Marahiel ◽  
T. Martin Schmeing
Keyword(s):  
Peptide Synthesis ◽  
Active Sites ◽  
Mutational Analysis ◽  
Bond Formation ◽  
Amide Bond ◽  
Active Site Residues ◽  
Nonribosomal Peptide ◽  
Amide Bond Formation ◽  
Catalytic Mechanisms ◽  
Insight Into

Nonribosomal peptide synthetases (NRPSs) are a family of multidomain, multimodule enzymes that synthesize structurally and functionally diverse peptides, many of which are of great therapeutic or commercial value. The central chemical step of peptide synthesis is amide bond formation, which is typically catalyzed by the condensation (C) domain. In many NRPS modules, the C domain is replaced by the heterocyclization (Cy) domain, a homologous domain that performs two consecutive reactions by using hitherto unknown catalytic mechanisms. It first catalyzes amide bond formation, and then the intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and the backbone carbonyl carbon to form a thiazoline, oxazoline, or methyloxazoline ring. The rings are important for the form and function of the peptide product. We present the crystal structure of an NRPS Cy domain, Cy2 of bacillamide synthetase, at a resolution of 2.3 Å. Despite sharing the same fold, the active sites of C and Cy domains have important differences. The structure allowed us to probe the roles of active-site residues by using mutational analyses in a peptide synthesis assay with intact bacillamide synthetase. The drastically different effects of these mutants, interpreted by using our structural and bioinformatic results, provide insight into the catalytic mechanisms of the Cy domain and implicate a previously unexamined Asp-Thr dyad in catalysis of the cyclodehydration reaction.

Peptide synthesis by prior thiol capture. 4. Amide bond formation. The effect of a side-chain substituent on the rates of intramolecular O,N-acyl transfer

1986 ◽  
Vol 51 (17) ◽  
pp. 3320-3324 ◽  
Author(s):  
D. S. Kemp ◽  
Nicholas G. Galakatos ◽  
Stanley Dranginis ◽  
Christopher Ashton ◽  
Nader Fotouhi ◽  
...  
Keyword(s):  
Peptide Synthesis ◽  
Bond Formation ◽  
Amide Bond ◽  
Acyl Transfer ◽  
Side Chain ◽  
Amide Bond Formation
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