Synthesis and biological properties of 4-norleucine-neuropeptide Y; secondary structure of neuropeptide Y.

Neuropeptide Y (NPY) is a 36 amino acid peptide amide isolated from porcine brain. The NPY analog, 4-norleucine-NPY was synthesized by a solid-phase method and purified to homogeneity in 20% yield by reverse-phase chromatography. Investigation of the biological properties indicated that the analog is an agonist of NPY. Secondary structural analyses revealed that NPY and the analog exhibited predominantly alpha-helical and beta-sheet structures, respectively; however, experiments in trifluoroethanol indicated that the analog has the potential of assuming an alpha-helical structure. Based on circular dichroism (CD), Raman spectroscopy and Chou-Fasman analyses, a model has been proposed for the secondary structure of NPY.

Serum lipid effects of a high-monounsaturated fat diet based on macadamia nuts.

BACKGROUND: Recent studies have identified potential beneficial effects of eating nuts, most of which have substantial amounts of monounsaturated fats. Macadamia nuts are 75% fat by weight, 80% of which is monounsaturated. OBJECTIVE: To examine variations in serum lipid levels in response to a high-monounsaturated fat diet based on macadamia nuts. METHODS: A randomized crossover trial of three 30-day diets was conducted in 30 volunteers aged 18 to 53 years from a free-living population. Each was fed a "typical American" diet high in saturated fat (37% energy from fat); an American Heart Association Step 1 diet (30% energy from fat); and a macadamia nut-based monounsaturated fat diet (37% energy from fat) in random order. Serum total cholesterol, high-density lipoprotein cholesterol, and triglyceride levels were measured. RESULTS: Mean total cholesterol level after the typical American diet was 5.20 mmol/L (201 mg/dL). After the Step 1 diet and the macadamia nut diet, total cholesterol level was 4.99 mmol/L (193 mg/dL) and 4.95 mmol/L (191 mg/dL), respectively. Low-density lipoprotein cholesterol level was 3.37 mmol/L (130 mg/dL) (typical diet), 3.21 mmol/L (124 mg/dL) (Step 1 diet), and 3.22 mmol/L (125 mg/dL) (macadamia nut diet). High-density lipoprotein cholesterol level was 1.43 mmol/L (55 mg/dL) (typical), 1.34 mmol/L (52 mg/dL) (Step 1), and 1.37 mmol/L (53 mg/dL) (macadamia nut). Lipid values after the Step 1 and macadamia nut diets were significantly different from those after the typical diet (P<.05). CONCLUSIONS: The macadamia nut-based diet high in monounsaturated fat and the moderately low-fat diet both had potentially beneficial effects on cholesterol and low-density lipoprotein cholesterol levels when compared with a typical American diet.

Non-uniform triple helical structure in chick skin type I collagen on thermal denaturation: Raman spectroscopic study.

The individual chains in the triple helix of collagen occur in a conformation related to polyproline II because of the presence of large number of imino peptide bonds. However, these residues are not evenly distributed in the collagen molecule which also contains many non-imino residues. These non-imino regions of collagen may be expected to show preference for other than triple helical conformations. The appearance of several Raman bands in solution phase at 65 degrees C raises the possibility of non-uniform triple helical structure in collagen. Raman spectroscopic studies on collagen in the solid state and in solution at a temperature greater than its denaturation temperature, reported here suggest that denatured collagen may exhibit an ensemble of conformational states with yet unknown implications to the biochemical interactions of this important protein component of connective tissues.

Human pancreatic thread protein, an exocrine thread protein with possible implications to Alzheimer's disease: secondary structure in solution at acid pH.

The secondary structure of human pancreatic thread protein (HPTP) in solution at acid pH was derived using Fourier transform infrared (FT-IR) and laser Raman spectroscopic studies. The experimentally derived secondary structure of HPTP was compared with the secondary structure obtained by the Chou-Fasman algorithm. Pancreatic thread protein is a major exocrine secretory protein that in vitro forms filamentous bundles reminiscent of the paired helical filaments of Alzheimer's disease (AD). PTP immunoreactivity in brains afflicted with AD has been demonstrated previously and high levels of its mRNA in the developing human brain have also been reported in the literature. The above studies suggest that AD is associated with enhanced expression of PTP-related transcripts with interneuronal accumulation of PTP-like proteins. The experimentally derived secondary structure of HPTP consists of a significant proportion of beta-sheets and beta-turns and lesser amounts of alpha-helical structures. The beta-sheet component presumably plays an important role in the pH-dependent globule-fibril transformation of HPTP leading to antiparallel beta-sheet structure in the aggregated state. The secondary structure of HPTP and its globule-fibril transformation lend credence to the belief that AD may be viewed as a conformational disease.

Conformational features of dynorphin A-(1-13), Laser Raman spectroscopic studies.

Conformational features of dynorphin A-(1-13) were examined by laser Raman spectroscopy. Dynorphin A-(1-13) appears to have a mixture of extended beta-pleated sheet and "random" structure.