Abstract
Various procedures for synthesis of peptides by Boc and Fmoc-based methods are described. Synthesis of depsipeptides and N-terminal hydroxyl peptide synthesis are illustrated. The various peptides are characterised by mass spectrometry and analytical HPLC. The rate constant for the dissociation of the respective prodrugs can be studied by chromatographic procedures. The concentrations of the prodrug and the drug can be estimated from their peak areas respectively. The first-order dissociation rate constants of the prodrugs can be determined by plotting the logarithm of the concentration of the prodrug at various time intervals. Peptides can be purified using preparative HPLC and purified peptides can be used for luciferase–based bioassays to study the activity of the various prodrugs. Detailed bioassays to examine the conversion of the prodrug to the drug under therapeutic conditions are described.
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References
Schnolzer M et al (1992) Int J Pept Protein Res 40(3–4):180–193
Personal Communications with Prof. Phil Dawson . Scripps Research Institute, San Diego, California
Williams C (2004) Nature Reviews. Drug Discovery 3:125–135
Samantha EG, Peter JB, Louise HN (1997) J Biomol Screen 2(4):235–240
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De, A. (2013). Experimental Procedures. In: Application of Peptide-Based Prodrug Chemistry in Drug Development. SpringerBriefs in Pharmaceutical Science & Drug Development. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-4875-4_3
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DOI: https://doi.org/10.1007/978-1-4614-4875-4_3
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