Applications of Chemical Ligation in Peptide Synthesis via Acyl Transfer

2014 ◽  
pp. 229-265 ◽  
Author(s):  
Siva S. Panda ◽  
Rachel A. Jones ◽  
C. Dennis Hall ◽  
Alan R. Katritzky
Keyword(s):  
Peptide Synthesis ◽  
Acyl Transfer ◽  
Chemical Ligation

Derivatized Amino Acids Relevant to Native Peptide Synthesis by Chemical Ligation and Acyl Transfer

2003 ◽  
Vol 68 (24) ◽  
pp. 9247-9254 ◽  
Author(s):  
Derrick L. J. Clive ◽  
Soleiman Hisaindee ◽  
Don M. Coltart
Keyword(s):  
Amino Acids ◽  
Peptide Synthesis ◽  
Acyl Transfer ◽  
Chemical Ligation ◽  
Native Peptide

scholarly journals Derivatized Amino Acids Relevant to Native Peptide Synthesis by Chemical Ligation and Acyl Transfer.

ChemInform ◽  
2004 ◽  
Vol 35 (13) ◽  
Author(s):  
Derrick L. J. Clive ◽  
Soleiman Hisaindee ◽  
Don M. Coltart
Keyword(s):  
Amino Acids ◽  
Peptide Synthesis ◽  
Acyl Transfer ◽  
Chemical Ligation ◽  
Native Peptide

scholarly journals Peptide Bond Synthesis by a Mechanism Involving an Enzymatic Reaction and a Subsequent Chemical Reaction

2015 ◽  
Vol 291 (4) ◽  
pp. 1735-1750 ◽  
Author(s):  
Tomoko Abe ◽  
Yoshiteru Hashimoto ◽  
Ye Zhuang ◽  
Yin Ge ◽  
Takuto Kumano ◽  
...  
Keyword(s):  
Peptide Synthesis ◽  
Chemical Reaction ◽  
Enzymatic Reaction ◽  
Amide Bond ◽  
Acyl Transfer ◽  
Native Chemical Ligation ◽  
Specific Substrate ◽  
Chemical Ligation ◽  
Subsequent Chemical Reaction ◽  
Subsequent Chemical

We recently reported that an amide bond is unexpectedly formed by an acyl-CoA synthetase (which catalyzes the formation of a carbon-sulfur bond) when a suitable acid and l-cysteine are used as substrates. DltA, which is homologous to the adenylation domain of nonribosomal peptide synthetase, belongs to the same superfamily of adenylate-forming enzymes, which includes many kinds of enzymes, including the acyl-CoA synthetases. Here, we demonstrate that DltA synthesizes not only N-(d-alanyl)-l-cysteine (a dipeptide) but also various oligopeptides. We propose that this enzyme catalyzes peptide synthesis by the following unprecedented mechanism: (i) the formation of S-acyl-l-cysteine as an intermediate via its “enzymatic activity” and (ii) subsequent “chemical” S → N acyl transfer in the intermediate, resulting in peptide formation. Step ii is identical to the corresponding reaction in native chemical ligation, a method of chemical peptide synthesis, whereas step i is not. To the best of our knowledge, our discovery of this peptide synthesis mechanism involving an enzymatic reaction and a subsequent chemical reaction is the first such one to be reported. This new process yields peptides without the use of a thioesterified fragment, which is required in native chemical ligation. Together with these findings, the same mechanism-dependent formation of N-acyl compounds by other members of the above-mentioned superfamily demonstrated that all members most likely form peptide/amide compounds by using this novel mechanism. Each member enzyme acts on a specific substrate; thus, not only the corresponding peptides but also new types of amide compounds can be formed.

Peptide synthesis by prior thiol capture—V. The scope and control of disulfide interchange during the acyl transfer step

1987 ◽  
Vol 28 (40) ◽  
pp. 4637-4640 ◽  
Author(s):  
D.S. Kemp ◽  
Nader Fotouhi
Keyword(s):  
Peptide Synthesis ◽  
Acyl Transfer ◽  
Transfer Step ◽  
And Control

scholarly journals Reinvestigation of a Critical Reductive Amination Step Leads to an Optimized Protocol for the Synthesis of N-2-Hydroxybenzylcysteine Peptide Crypto-Thioesters

2020 ◽  
Author(s):  
Skander Abboud ◽  
Vincent AUCAGNE
Keyword(s):  
Peptide Synthesis ◽  
Reaction Mechanisms ◽  
Reductive Amination ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Building Blocks ◽  
Native Chemical Ligation ◽  
Chemical Ligation ◽  
Optimized Protocol ◽  
Depth Study

An in-depth study of the Fmoc-based solid phase peptide synthesis of N-Hnb-Cys crypto-thioester peptides, advantageous building blocks for the native chemical ligation-based synthesis of proteins, led to the identification of epimerized and imidazolidinone side products formed during a key reductive amination step. The understanding of the underlying reaction mechanisms was crucial for the developement of an automatable optimized synthetic protocol.

Protease-catalyzed peptide synthesis using inverse substrates: The influence of reaction conditions on the trypsin acyl transfer efficiency

1991 ◽  
Vol 38 (1) ◽  
pp. 104-108 ◽  
Author(s):  
Volker Schellenberger ◽  
Hans-Dieter Jakubke ◽  
Nina P. Zapevalova ◽  
Yuri V. Mitin
Keyword(s):  
Peptide Synthesis ◽  
Acyl Transfer ◽  
Transfer Efficiency ◽  
Reaction Conditions

ChemInform Abstract: Native Chemical Ligation with Nα-Acyl Transfer Auxiliaries

ChemInform ◽  
2010 ◽  
Vol 41 (39) ◽  
pp. no-no
Author(s):  
John Offer
Keyword(s):  
Acyl Transfer ◽  
Native Chemical Ligation ◽  
Chemical Ligation

scholarly journals Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

2017 ◽  
Vol 8 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Hader E. Elashal ◽  
Yonnette E. Sim ◽  
Monika Raj
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Solid Support ◽  
Native Chemical Ligation ◽  
Selective Activation ◽  
Chemical Ligation ◽  
Peptide Thioester ◽  
Peptide Thioesters

Fmoc solid phase peptide synthesis of peptide thioesters by displacement of the cyclic urethane moiety obtained by the selective activation of C-terminal serine.

ChemInform Abstract: Peptide Synthesis by Prior Thiol Capture. Part 4. Amide Bond Formation: The Effect of a Side-Chain Substituent on the Rates of Intramolecular O,N-Acyl Transfer.

ChemInform ◽  
1987 ◽  
Vol 18 (8) ◽  
Author(s):  
D. S. KEMP ◽  
N. G. GALAKATOS ◽  
S. DRANGINIS ◽  
C. ASHTON ◽  
N. FOTOUHI ◽  
...  
Keyword(s):  
Peptide Synthesis ◽  
Bond Formation ◽  
Amide Bond ◽  
Acyl Transfer ◽  
Side Chain ◽  
Amide Bond Formation
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