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Amide Bond Activation of Biological Molecules

Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
Author to whom correspondence should be addressed.
Academic Editor: Michal Szostak
Molecules 2018, 23(10), 2615;
Received: 7 September 2018 / Revised: 9 October 2018 / Accepted: 9 October 2018 / Published: 12 October 2018
(This article belongs to the Special Issue Amide Bond Activation)


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. View Full-Text
Keywords: peptide bond cleavage; amide bond resonance; twisted amides; enzymes; metal complexes; catalysts peptide bond cleavage; amide bond resonance; twisted amides; enzymes; metal complexes; catalysts

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Mahesh, S.; Tang, K.-C.; Raj, M. Amide Bond Activation of Biological Molecules. Molecules 2018, 23, 2615.

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