De novo design of existing or novel peptide folds demand a thorough understanding of the rules that underlie protein structure and stability. The recurring theme in many design strategies is the use of amino acid propensities to adopt various secondary structures. There are many occasions in the literature where affinity is enhanced through hydrophobic interactions, even at the expense of hydrogen bonds. Literature data support the hypothesis that the balance of contribution between polar and hydrophobic interactions is determinant in molecular recognition. During the last twenty years a variety of "nonclassical" exogenous opioid peptides derived from enzymatic digest of various food protein sources has been demonstrated.[1] Most of the food-derived opioids are peptides fragments of milk proteins (caseins, ?-lactalbumin, ?-lactoglobulin, lactotransferrin).[2]. In our ongoing work with bioactive peptides derived from milk proteins[3] we have observed the structural, conformational, and dynamic properties of ?-lactorphin and ?-lactorphin, that derived from whey protein ?-lactalbumin and ?-lactoglobulin respectively. As found for ?-lactorphin also ?-lactorphin showed affinity for opioid receptors and was found to behave like a µ-opioid receptor agonist. We present here results of a NMR study of Boc- and -OMe protect analogues of ?-lactorphin and ?-lactorphin which provide useful informations about conformational behaviour in solution. Our interpretation has been aided by similar study of analogues containing conformational constrictions due to the presence of prolyl residue(s) and of dimeric octapeptide of ?-lactorphin. References 1.H.S. Gill, F.Doull, K.J. Rutherfurd, M.L.Cross British J. of Nutrition(2000) 84 (Suppl.1), S111-S117 2.H.Meisel Biopolymers (1997) 240, 119-128 E.Fenude, S.Dedola, M.Fais Congress "Complex Systems: structure,properties, reactivity, and dynamics"(2005) Alghero, 13-15/06/2005 3. G. Micera, D. Sanna, & al, Journal of Inorganic Biochemistry(1998) 69, 91-95
Conformational constraints in synthetic alfa- and beta-lactorphin
E Fenude;
2016
Abstract
De novo design of existing or novel peptide folds demand a thorough understanding of the rules that underlie protein structure and stability. The recurring theme in many design strategies is the use of amino acid propensities to adopt various secondary structures. There are many occasions in the literature where affinity is enhanced through hydrophobic interactions, even at the expense of hydrogen bonds. Literature data support the hypothesis that the balance of contribution between polar and hydrophobic interactions is determinant in molecular recognition. During the last twenty years a variety of "nonclassical" exogenous opioid peptides derived from enzymatic digest of various food protein sources has been demonstrated.[1] Most of the food-derived opioids are peptides fragments of milk proteins (caseins, ?-lactalbumin, ?-lactoglobulin, lactotransferrin).[2]. In our ongoing work with bioactive peptides derived from milk proteins[3] we have observed the structural, conformational, and dynamic properties of ?-lactorphin and ?-lactorphin, that derived from whey protein ?-lactalbumin and ?-lactoglobulin respectively. As found for ?-lactorphin also ?-lactorphin showed affinity for opioid receptors and was found to behave like a µ-opioid receptor agonist. We present here results of a NMR study of Boc- and -OMe protect analogues of ?-lactorphin and ?-lactorphin which provide useful informations about conformational behaviour in solution. Our interpretation has been aided by similar study of analogues containing conformational constrictions due to the presence of prolyl residue(s) and of dimeric octapeptide of ?-lactorphin. References 1.H.S. Gill, F.Doull, K.J. Rutherfurd, M.L.Cross British J. of Nutrition(2000) 84 (Suppl.1), S111-S117 2.H.Meisel Biopolymers (1997) 240, 119-128 E.Fenude, S.Dedola, M.Fais Congress "Complex Systems: structure,properties, reactivity, and dynamics"(2005) Alghero, 13-15/06/2005 3. G. Micera, D. Sanna, & al, Journal of Inorganic Biochemistry(1998) 69, 91-95I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
