ChemInform Abstract: T3P (Propylphosphonic Anhydride) Mediated Conversion of Nα-Protected Amino/Peptide Acids into Thioacids.

ChemInform ◽  
2012 ◽  
Vol 43 (27) ◽  
pp. no-no
Author(s):  
Chilakapati Madhu ◽  
Basavaprabhu Basavaprabhu ◽  
T. M. Vishwanatha ◽  
Vommina V. Sureshbabu
Keyword(s):  
Peptide Acids

Efficient, racemization-free amidation of protected peptide acids with precise stereochemical purity control

Peptides 1994 ◽  
1995 ◽  
pp. 197-198
Author(s):  
Gy. Szókán ◽  
Cs. Somlai ◽  
B. Penke ◽  
K. Krizsán ◽  
M. Almás
Keyword(s):  
Peptide Acids ◽  
Purity Control

Robust synthesis of C-terminal cysteine-containing peptide acids through a peptide hydrazide-based strategy

2019 ◽  
Vol 17 (23) ◽  
pp. 5698-5702 ◽  
Author(s):  
Chao Zuo ◽  
Bing-Jia Yan ◽  
Han-Ying Zhu ◽  
Wei-Wei Shi ◽  
Tong-Kuai Xi ◽  
...  
Keyword(s):  
Efficient Strategy ◽  
Highly Efficient ◽  
Peptide Acids ◽  
Robust Synthesis

A simple-to-operate and highly efficient strategy for the epimerization-free synthesis of C-terminal Cys-containing peptide acids, which avoids the use of derivatization reagents for resin modification, is developed.

ChemInform Abstract: Epimerization-Free Amidation of Protected Peptide Acids

ChemInform ◽  
2010 ◽  
Vol 26 (45) ◽  
pp. no-no
Author(s):  
C. SOMLAI ◽  
G. SZOKAN ◽  
B. PENKE
Keyword(s):  
Peptide Acids

A useful method for the preparation of fully protected peptide acids and esters

1997 ◽  
Vol 38 (8) ◽  
pp. 1279-1282 ◽  
Author(s):  
André Pichette ◽  
Normand Voyer ◽  
Rémi Larouche ◽  
Jean-Christophe Meillon
Keyword(s):  
Peptide Acids

scholarly journals An Efficient and Epimerization Free Synthesis of C-Terminal Arylamides Derived from α-Amino Acids and Peptide Acids via T3P Activation

2014 ◽  
Vol 20 (3) ◽  
pp. 353-363 ◽  
Author(s):  
Chilakapati Madhu ◽  
Panguluri NageswaraRao ◽  
N. Narendra ◽  
Vommina V. Sureshbabu
Keyword(s):  
Amino Acids ◽  
Peptide Acids

Solid-Phase Synthesis of Selectively Protected Peptides: Use of Thallous Alkoxide as Catalyst in the Transesterification Step

1974 ◽  
Vol 52 (15) ◽  
pp. 2832-2839 ◽  
Author(s):  
J. Y. Savoie ◽  
Moira A. Barton
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Butyl Ester ◽  
Side Reaction ◽  
Ester Group ◽  
Phase Synthesis ◽  
Large Molecules ◽  
Merrifield Resin ◽  
Peptide Acids ◽  
Protected Peptides

Transesterification with 2-dimethylaminoethanol, in the presence of thallous alkoxide, was found to provide a useful method for the cleavage of protected peptides from the Merrifield resin after solid-phase synthesis. The extent of racemization, at the C-terminal residue, was low (< 1%) in the case of peptides containing C-terminal alanine or valine residues. The method was also found to provide good yields of the protected peptide derivative even in the case of the severely sterically hindered C-terminal valine peptides. A study of the α → β aspartyl transpeptidation, showed that the extent of this side reaction was low (< 1% β-isomer) in the case of the labile α-aspartylglycine sequence, when a short transesterification time was employed. The t-butyl ester group was shown to be stable under the conditions of transesterification and this group is recommended for the protection of carboxylic acid side chains. Hydrolysis of the 2-dimethylaminoethyl esters was accomplished by treatment with water or dilute base, to yield the selectively protected peptide acids, suitable for use as building units in the synthesis of large molecules by solid-phase or solution techniques.

scholarly journals Amide Bond Activation of Biological Molecules

Molecules ◽  
2018 ◽  
Vol 23 (10) ◽  
pp. 2615 ◽  
Author(s):  
Sriram Mahesh ◽  
Kuei-Chien Tang ◽  
Monika Raj
Keyword(s):  
Organic Molecules ◽  
Unique Feature ◽  
Bond Activation ◽  
Three Dimensional ◽  
Review Article ◽  
Biological Molecules ◽  
Amide Bond ◽  
Amide Bonds ◽  
Dna And Rna ◽  
Peptide Acids

Amide bonds are the most prevalent structures found in organic molecules and various biomolecules such as peptides, proteins, DNA, and RNA. The unique feature of amide bonds is their ability to form resonating structures, thus, they are highly stable and adopt particular three-dimensional structures, which, in turn, are responsible for their functions. The main focus of this review article is to report the methodologies for the activation of the unactivated amide bonds present in biomolecules, which includes the enzymatic approach, metal complexes, and non-metal based methods. This article also discusses some of the applications of amide bond activation approaches in the sequencing of proteins and the synthesis of peptide acids, esters, amides, and thioesters.

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