Structural determinants conferring unusual long life in human serum to rattlesnake-derived antimicrobial peptide Ctn[15-34].

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ID: 3062
2019
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Abstract
Ctn[15-34], a downsized version of the snake venom cathelicidin-like peptide crotalicidin (Ctn), shows an unusually high lifespan (t , approximately 12 h) in human serum, which significantly adds to its promise as an antimicrobial and antitumor agent. Herein we investigate the role of Ctn[15-34] structure on serum survival. Using a set of analogs, we show that C-terminal amidation, as well as the specific layout of the Ctn[15-34] sequence-a helical N-terminal domain followed by a hydrophobic domain-is crucial for slow degradation, and any change in their arrangement results in significantly lower t . Aside from the privileged primary structure, features such as self-aggregation can be ruled out as causes for the long serum life. Instead, studies in other protease-rich fluids suggest a key role for certain human serum components. Finally, we demonstrate that Ctn[15-34] is able to induce bacterial death even after 12-hour pre-incubation in serum, in agreement with the proteolytic data. Altogether, the results shed light on the uncommon stability of Ctn[15-34] in human serum and confirm its potential as an anti-infective lead.
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prezpeinado2019structuraljournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Pérez-Peinado, Clara;Dias, Susana A;Mendonça, Diogo A;Castanho, Miguel A R B;Veiga, Ana S;Andreu, David;
Journal journal of peptide science : an official publication of the european peptide society
Year 2019
DOI
10.1002/psc.3195
URL
Keywords Keywords not found

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