Jenifer Malia*
This study presents a successful modification technique for engineering multifunctional peptides derived from a Kunitz family trypsin inhibitory peptide. By incorporating specific amino acid substitutions and structural modifications, the peptides were endowed with enhanced stability, binding affinity, and bioactivity. The modified peptides demonstrated significant inhibition of trypsin as well as additional functional properties, such as antimicrobial and anti-inflammatory activities. Structural analyses confirmed the maintenance of the Kunitz domain's integrity, ensuring the preservation of its inhibitory function. This approach provides a robust framework for developing versatile peptide-based therapeutics with multiple biological activities.
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