Abstract
The main goal of structure-activity relationship studies in bioactive peptides, relevant to medicinal chemistry, is the understanding of the biological phenomena at molecular level in order to produce and possibly develop new materials which might mimic biological processes by enhancing or somehow modulating their effects. The peptide pharmaceutical targets are usually hormones, enzymes, transport systems, neurotransmitters, ion channel ionophores antibiotics, antigens. The advantages in the use of peptides as pharmaceuticals are based on the fact that: (i) they should be considered “natural” products; (ii) opportunely modified analogs could possibly show increased potency and enhanced specificity; (iii) they are easy to synthesize and (iv) they could present extraordinary ranges of biological properties coupled with minimal non-mechanism-based toxicity. In this area, constrained non-coded α-amino acid residues are of great interest as “building blocks” for the preparation of analogs, which should not only retain the pharmacological properties of the native peptide, but they should also exhibit enhanced resistance to biodegradation with improved bioavailability and pharmacokinetics.
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Benedetti, E. (1994). Molecular Engineering in the Preparation of Bioactive Peptides. In: Doniach, S. (eds) Statistical Mechanics, Protein Structure, and Protein Substrate Interactions. NATO ASI Series, vol 325. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1349-4_33
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