CLONING AND PLANT-EXPRESSION DESIGN STRATEGIES FOR HUMAN ANTIMICROBIAL PEPTIDES: LL-37 AND DERMCIDIN AS CASE STUDIES
DOI:
https://doi.org/10.64013/bbasrjlifess.v2026i1.54Keywords:
Antimicrobial peptides; LL-37; Dermcidin; Plant molecular farming; pCAMBIA2301; Binary vector; Cloning strategy; Recombinant expressionAbstract
The emergence of antimicrobial resistance (AMR) has added to the search for alternatives to antibiotics. Antimicrobial peptide (AMP) is an attractive antimicrobial agent due to its combination of broad antimicrobial effects with other qualities of biomodulation of immune function and antimicrobial control of biofilms. The present review explores the comparison of the use of plant-based recombinant expression as an alternative to the use of human AMPs in bioethics, using the example of LL-37 and Dermcidin. LL-37 is a Cationic, amphipathic host-defense peptide with membrane-active, antibiofilm, antiviral, and immunomodulatory functions, whereas the peptides that result during fermentation by Dermcidin are typified by DCD-1L, which is an anionic, Dcd-derived secretory peptide. Investigating pCAMBIA2301 as a representative binary-vector construct, the review highlights peptide-specific construct planning, codon optimization, regulatory context, targeting, stabilization, and recovery. The general thesis is that the production of these peptides by plants necessitates that peptide biology be integrated with expression-system engineering instead of simply inserting a peptide-coding sequence into a vector.
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