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Activities of Synthetic Host Defense Propeptides Processed by Neutrophil Elastase - Book Report/Review Example

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The reporter states that the research on antimicrobial peptides (AMP) has received a lot of scholarly attention with the major focus on the respiratory system. Since the initial findings in 1996 that epithelia present in the linings of the respiratory airways of patients suffering from cystic fibrosis did not eliminate the bacteria…
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Activities of Synthetic Host Defense Propeptides Processed by Neutrophil Elastase
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Download file to see previous pages Owing to the challenges encountered in sampling the airway surface fluid (ASF), studies on airway peptides have been limited to in vitro experiments (Devine and Hancock 2004). This report is based on an article titled In Vitro Activities of Synthetic Host Defense Propeptides Processed by Neutrophil Elastase against Cystic Fibrosis Pathogens authored in May 2011 by a team of fifteen researchers led by Stephane Desgrandes of the Centre for Synthesis and Chemical Biology; Royal College of Surgeons in Ireland. The article was published in the Antimicrobial Agents and Chemotherapy Journal which is affiliated to the American Society for Microbiology.
The general objective of the research was to investigate whether the antimicrobial and hemolytic actions of host defense peptides can be stringently controlled through its modification as propeptide. The study was focused on investigating the whether the natural defense mechanisms of the host defense peptides (HDP) can be used to develop a prodrug analogy utilizing neutrophil elastase (NE)against the pathogens involved in Cystic Fibrosis (CF).
It is essential to understand the structural and biochemical characteristics and importance of peptides as they are the fundamental components of the research. Peptides are biochemically active chemical compounds made up of amino acids consisting of an amide group between a carboxyl and an amine group in different amino acids. Peptides are joined together by peptide bonds and are named according to the number of peptide bonds forming the peptide chain. Peptides consisting of less than twenty peptide bonds are termed as oligopeptides while those with more than twenty peptide bonds are called polypeptides (Jens-Michael and Kabelitz 2005). There is controversy as to the size of peptides that qualifies it to become a protein.  Depending on their characteristic features and the nature of the amino acids constituting them, peptides can be classified as either L-peptides or D-peptides. L-peptides are derived from amino acids which occur naturally and are degradable by enzymes while D-peptides are derived from artificial amino acids and are not degradable by enzymes (Devine and Hancock 2004). ...Download file to see next pagesRead More
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