alexa Protease-mediated peptide bond formation. On some unexpected outcomes during enzymatic synthesis of leu-enkephalin.
Chemical Engineering

Chemical Engineering

Journal of Chemical Engineering & Process Technology

Author(s): Kullmann W

Abstract Share this page

Abstract In the course of a study in protease-controlled peptide synthesis, several promising pathways to synthetic enkephalins had to be discarded or modified because they failed to give the required products. Partial deprotection of peptide fragments prior to chain elongation resulted in an enhanced susceptibility of scissile bonds to proteolysis. The use of proteases, the specificity of which was not confined solely to the bond to be synthesized, thus led to a priori cleavage of pre-existing peptide bonds. Subsequently, enzyme-mediated synthesis of new peptide bonds between initial reactants and nascent degradation products furnished undesired, often truncated peptides. A detailed characterization of the undesired products gave information as to whether or not the peptide bonds were susceptible to proteolytic cleavage or accessible via enzymatic synthesis. In this way, the unexpected outcome of protease catalysis led to working predictions regarding enzyme-mediated peptide bond formation, and thus, finally contributed to the successful synthesis of the target peptides.
This article was published in J Biol Chem and referenced in Journal of Chemical Engineering & Process Technology

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords