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We are intrigued by the structural complexity of naturally cyclic and entangled peptides. Such 'miniproteins' often exhibit improved metabolic and thermal stability relative to their acyclic sequences. These structural archetypes may serve as scaffolds for the display of incorporated inhibitors (or recognition sequences) and could ultimately serve as constructs for novel peptide therapeutics.
DESIGN, MIMIC & SYNTHESIS OF CHALLENGING PEPTIDIC STRUCTURES
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