Encrypted Antimicrobial Peptides from Plant Proteins

May 22, 2018

Title

Encrypted Antimicrobial Peptides from Plant Proteins

Author

M. H. S. Ramada, G. D. Brand, F. Y. Abrão, M. Oliveira, J. L. Cardozo Filho, R. Galbieri, K. P. Gramacho, M. V. Prates, C. Bloch, Jr

Year

2017

Journal

Scientific Reports

Abstract

Examples of bioactive peptides derived from internal sequences of proteins are known for decades. The great majority of these findings appear to be fortuitous rather than the result of a deliberate and methodological-based enterprise. In the present work, we describe the identification and the biological activities of novel antimicrobial peptides unveiled as internal fragments of various plant proteins founded on our hypothesis-driven search strategy. All putative encrypted antimicrobial peptides were selected based upon their physicochemical properties that were iteratively selected by an in-house computer program named Kamal. The selected peptides were chemically synthesized and evaluated for their interaction with model membranes. Sixteen of these peptides showed antimicrobial activity against human and/or plant pathogens, some with a wide spectrum of activity presenting similar or superior inhibition efficacy when compared to classical antimicrobial peptides (AMPs). These original and previously unforeseen molecules constitute a broader and undisputable set of evidences produced by our group that illustrate how the intragenic concept is a workable reality and should be carefully explored not only for microbicidal agents but also for many other biological functions.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Membrane interactions, Biochemistry