Abstract
Among the many molecular entities suitable for therapeutic use, peptides have emerged as a particularly attractive option for academic drug discovery and development. Their modular structure and extendibility, the availability of powerful and affordable screening platforms, and the relative ease-of-synthesis render therapeutic peptides highly approachable for teaching and research alike. With a strong focus on the therapeutic modulation of host defence pathways, including the complement and renin-angiotensin systems, the Molecular Pharmacy group at the University of Basel strongly relies on peptides to introduce students to practical aspects of modern drug design, to discover novel therapeutics for immune and inflammatory diseases, and to expand on options for the preclinical development of a promising drug class. Current projects reach from student-driven iterative design of peptidic angiotensin-converting enzyme inhibitors and the use of phage display technology to discover novel immune modulators to the development of protective peptide coatings for biomaterials and transplants and the structure-activity-relationship-guided optimization of therapeutic peptide drug candidates in late-stage clinical trials. Even at the current stage, peptides allow for a perfect circle between pharmaceutical research and education, and the recent spark of clinical applications for peptide-based drugs may only increase the value and relevance of this versatile drug class.
Highlights
Among the many molecular entities suitable for therapeutic use, peptides have emerged as a attractive option for academic drug discovery and development
Situated between low-molecular-weight (LMW) drugs and ‘biologics’ such as antibodies, therapeutic peptides represent a versatile class of pharmaceutical compounds consisting of amino acid chains.[1]
Chemical synthesis and biotechnology allowed for the rational design, de novo synthesis and large-scale production of peptidic drugs, leading to the approval of more than 100 therapeutic peptides spanning various clinical indications.[2]
Summary
Situated between low-molecular-weight (LMW) drugs and ‘biologics’ such as antibodies, therapeutic peptides represent a versatile class of pharmaceutical compounds consisting of amino acid chains (usually less than 40 residues).[1]. In vitro selection methods, such as phage and mRNA display, enable the generation of large peptide libraries for screening purposes.[3] Since its first report,[4] phage display has evolved into an accelerator of hit generation for both antibody and peptide drugs.[5] The library is displayed on an outer membrane protein of the phage, such as pIII or pVIII, and can reach a diversity of >109 molecules. The use of in vitro transcription and translation allows for easy incorporation of noncanonical amino acids and avoids transformation steps that can limit the diversity of phage libraries.[7]. Their high clinical relevance, accessibility and affordability greatly facilitates an integration of peptide drugs into the practical training of students while, at the same time, enabling academic drug discovery (Fig. 1).
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