Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 25, Issue 8, Pages -Publisher
WILEY
DOI: 10.1002/psc.3195
Keywords
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Funding
- Fundação para a Ciência e a Tecnologia [PTDC/QEQ-MED/4412/2014] Funding Source: FCT
- EU Marie Skłodowska-Curie Research and Innovation Staff Exchange (RISE) [644167] Funding Source: Medline
- Fundação para a Ciência e a Tecnologia [PTDC/QEQ-MED/4412/2014] Funding Source: Medline
- Spanish Ministry of Economy and Competitiveness (MINECO) [MDM-2014-0370, AGL2017-84097-C2-2-R, AGL2014-52395-C2, SAF2011-24899] Funding Source: Medline
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Ctn[15-34], a downsized version of the snake venom cathelicidin-like peptide crotalicidin (Ctn), shows an unusually high lifespan (t(1/2), 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(1/2). 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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