Derivatives of N-amidinoproline and their use in conventional and solid phase peptide synthesis

• Published in: Bioorganicheskaia khimiia Vol. 32; no. 6; p. 565
• Main Authors: Burov, S V, Moskalenko, Iu E, Leko, M V, Dorosh, M Iu, Panarin, E F
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-11-2006
• Subjects: Dipeptides - chemical synthesis; Dipeptides - chemistry; Fibrinogen - chemistry; Nuclear Magnetic Resonance, Biomolecular - methods; Peptides - chemical synthesis; Peptides - chemistry; Proline - analogs & derivatives; Proline - chemistry; Protein Structure, Secondary; Spectrometry, Mass, Electrospray Ionization - methods
• ISSN: 0132-3423

N-Amidinoproline, a hybrid structure modeling key features of the Arg-Pro sequence, was synthesized. The activation of carboxyl group of free N-amidinoproline was found to result in the formation of a cyclic side product, whose structure was confirmed by ESI MS, 1H NMR, and 13C NMR spectra. The preparation of N-(mesitylenesulfonylamidino)-L-proline using the mesitylenesulfonyl derivative of 2-methylisourea was demonstrated to be accompanied by partial racemization. The target product was synthesized by modification of N-amidinoproline by mesitylenesulfonyl chloride. The possibility of using N-amidinoproline in the N-terminal modification of a peptide chain was shown by the example of synthesis of an analogue of the 95-98 fragment of fibrinogen alpha chain.