Abstract
The complement system and antimicrobial peptides (AMPs) are known to be vital humoral factors of innate immunity. Earlier we showed the double-sided influence of arenicin-1 (Ar-1), the AMP from a sea polychaeta Arenicola marina, on the complement activation. In this work we studied the binding of Ar-1 to C3b protein, the fragment of the central complement component C3, using surface plasmon resonance. We also performed molecular docking and molecular dynamics of interaction between C3b fragment - C3c - and Ar-1. All these data showed that the influence of Ar-1 on complement activation might be realized through the interaction with C3b, the most important component for complement activation. Ar-1 may be used for the design of new complement regulators for treating complement-related diseases.
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