Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator
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Antimicrobial peptides (AMPs) are not only cytotoxic towards host pathogens or cancer cells but
also are able to act as immunomodulators. It was shown that some human and non-human AMPs can
interact with complement proteins and thereby modulate complement activity. Thus, AMPs could be
considered as the base for complement-targeted therapeutics development. Arenicins from the sea
polychaete Arenicola marina, the classical example of peptides with a β-hairpin structure
stabilized by a disulfide bond, were shown earlier to be among the most prospective regulators.
Here, we investigate the link between arenicins' structure and their antimicrobial, hemolytic
and complement-modulating activities using the derivative Ar-1-(C/A) without a disulfide bond.
Despite the absence of this bond, the peptide retains all important functional activities and
also appears less hemolytic in comparison with the natural forms. These findings could help to
investigate new complement drugs for regulation using arenicin derivatives.
Reference
Krenev, I. A., Umnyakova, E. S., Eliseev, I. E., Dubrovskii, Y. A., Gorbunov, N. P., Pozolotin, V. A., ... & Berlov, M. N. (2020). Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator. Marine Drugs, 18(12), 631.
For Research Use Only.
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