Glycosylation Significantly Modifies LL-37 Fragment's Structure and Biological Activity

LL-37 is the sole human cathelicidin, a crucial component of the innate immune system, known for its broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. Beyond direct pathogen killing, LL-37 also possesses significant immunomodulatory properties, influencing inflammation, wound healing, and angiogenesis. The C-terminal fragment of LL-37 retains much of this biological activity, making it a promising candidate for therapeutic development. However, the precise impact of post-translational modifications, specifically N- and O-glycosylation, on the structural integrity and diverse biological functions of this C-terminal LL-37 fragment has not been thoroughly elucidated. Understanding these modifications is vital for optimizing its therapeutic potential.