Many biologically active peptides are generated by proteolytic processing of various higher molecular weight multifunctional precursor peptides and proteins. The enzymes of different structures and specificity are involved in the synthesis, posttranslational modifications and release of peptide products, including hormones, neurotransmitters, and opioids. During the last two decades a variety of "atypical" exogenous opioid peptides derived from enzymatic digest of various food proteins sources has been demonstrated. Most of the food-derived opioids are peptides fragments of milk proteins (caseins, alpha-lactalbumin, beta-lactoglobulin, and lactotransferrin), plant proteins (wheat gluten) or constituents of meats (hemoglobin and bovine serum albumin). These peptides identified in exogenous sources were named exorphins. Most of the information available so far has been collected about exorphins isolated from alpha- or beta-casein, casomorphins (CM-7, Tyr-Pro-Phe-Pro-Gly-Pro-Ile). Five opioid peptides were derived from the wheat gluten: Gly- Tyr-Tyr-Pro-Thr, Gly- Tyr-Tyr-Pro, Tyr-Gly- Gly-Trp-Leu, Tyr-Gly- Gly-Trp, Tyr-Pro-Ile-Ser-Leu, which were named gluten exorphins A5, A4, B5, B4, and C respectively. A series of "nonclassical" endogenous peptides (hemorphins) have been identified in the course of the study of proteolytic fragments of bovine blood hemoglobin. The primary structure determined by Edman degradation (Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe) corresponded to the fragment (31-40) of bovine hemoglobin beta-chain (LVV-hemorphin-7). In this work we have observed tetra- and penta-peptides fragments of N-terminal protected exorphins. These products have been synthesized, purified and then analyzed by NMR spectroscopy in order to obtain structural and conformational informations to use in molecular simulation experiments. A comparison of experimental spectroscopic data with structural information from empirical models allow us to understand behaviour of these peptides in solution. References 1.Fenude E. Dedola S., Fais M.., Computer simulation and conformational study performed by NMR in solution of oligopeptides fragments of N-terminal protected beta-casomorphines, VII Convegno "Complex Systems: structure, properties, reactivity and dynamics, Alghero, 13-15 Giugno 2005 2.Fanciulli G, Azara E, Wood TD, Dettori A, Delitala G, Marchetti M., Quantification of Gluten Exorphin A5 in cerebrospinal fluid by liquid chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 833(2):204-9. Epub 2006 Feb 28 3.Fenude E., Villano R., Studio sintetico e caratteristiche conformazionali di peptidi di interesse biomedico, SardiniaChem2008 Giornata di Studio Dedicata alla Chimica Organica delle Molecole Biologicamente Attive, 30 Maggio 2008 Sassari 4.Artenova N.V., Bumagina Z.M., Kasakov A.S., Shubin V.V., Gurvits B.Ya., Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins. Peptides, 31, 332-338, 2010
Conformational Behavior and Properties of Bioactive Peptides Derived from Food Proteins
Fenude Emma
2015
Abstract
Many biologically active peptides are generated by proteolytic processing of various higher molecular weight multifunctional precursor peptides and proteins. The enzymes of different structures and specificity are involved in the synthesis, posttranslational modifications and release of peptide products, including hormones, neurotransmitters, and opioids. During the last two decades a variety of "atypical" exogenous opioid peptides derived from enzymatic digest of various food proteins sources has been demonstrated. Most of the food-derived opioids are peptides fragments of milk proteins (caseins, alpha-lactalbumin, beta-lactoglobulin, and lactotransferrin), plant proteins (wheat gluten) or constituents of meats (hemoglobin and bovine serum albumin). These peptides identified in exogenous sources were named exorphins. Most of the information available so far has been collected about exorphins isolated from alpha- or beta-casein, casomorphins (CM-7, Tyr-Pro-Phe-Pro-Gly-Pro-Ile). Five opioid peptides were derived from the wheat gluten: Gly- Tyr-Tyr-Pro-Thr, Gly- Tyr-Tyr-Pro, Tyr-Gly- Gly-Trp-Leu, Tyr-Gly- Gly-Trp, Tyr-Pro-Ile-Ser-Leu, which were named gluten exorphins A5, A4, B5, B4, and C respectively. A series of "nonclassical" endogenous peptides (hemorphins) have been identified in the course of the study of proteolytic fragments of bovine blood hemoglobin. The primary structure determined by Edman degradation (Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe) corresponded to the fragment (31-40) of bovine hemoglobin beta-chain (LVV-hemorphin-7). In this work we have observed tetra- and penta-peptides fragments of N-terminal protected exorphins. These products have been synthesized, purified and then analyzed by NMR spectroscopy in order to obtain structural and conformational informations to use in molecular simulation experiments. A comparison of experimental spectroscopic data with structural information from empirical models allow us to understand behaviour of these peptides in solution. References 1.Fenude E. Dedola S., Fais M.., Computer simulation and conformational study performed by NMR in solution of oligopeptides fragments of N-terminal protected beta-casomorphines, VII Convegno "Complex Systems: structure, properties, reactivity and dynamics, Alghero, 13-15 Giugno 2005 2.Fanciulli G, Azara E, Wood TD, Dettori A, Delitala G, Marchetti M., Quantification of Gluten Exorphin A5 in cerebrospinal fluid by liquid chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 833(2):204-9. Epub 2006 Feb 28 3.Fenude E., Villano R., Studio sintetico e caratteristiche conformazionali di peptidi di interesse biomedico, SardiniaChem2008 Giornata di Studio Dedicata alla Chimica Organica delle Molecole Biologicamente Attive, 30 Maggio 2008 Sassari 4.Artenova N.V., Bumagina Z.M., Kasakov A.S., Shubin V.V., Gurvits B.Ya., Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins. Peptides, 31, 332-338, 2010I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
