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Blood, peptide research

At first glance, blood is the ideal sample from which to obtain a representative clinical sample suitable for peptide research. However, its complexity and the high abundance of certain proteins, such as albumin, fibrinogen, and immunoglobulins, render blood probably the most difficult of all proteomic samples... [Pg.118]

General trends in radiopharmaceutical research emphasize the use of small peptides. These molecules, of which the agents mentioned for thrombosis localization are an example, exhibit rapid and specific binding, and rapid blood clearance, two important parameters for a successflil radiopharmaceutical. Peptides are readily labeled with Tc and lend themselves to formulation as lyophilized kits that can be rapidly and rehably reconstituted. Possible targets for these molecules are quite varied, ranging from atherosclerotic plaque to P-amyloid (for Alzheimer s disease), to a variety of somatic receptors the populations of which are increased or decreased in disease. [Pg.485]

The vascular endothelium produces a number of substances that are released basally into the blood vessel wall to alter vascular smooth muscle tone. One such substance is endothelin (ET-1). Endothelin exerts its effects throughout the body, causing vasoconstriction as well as positive inotropic and chronotropic effects on the heart. The resulting increases in TPR and CO contribute to an increase in MAP. Synthesis of endothelin appears to be enhanced by many stimuli, including Ag II, vasopressin, and the mechanical stress of blood flow on the endothelium. Synthesis is inhibited by vasodilator substances such as prostacyclin, nitric oxide, and atrial natriuretic peptide. There is evidence that endothelin is involved with the pathophysiology of many cardiovascular diseases, including hypertension, heart failure, and myocardial infarction. Endothelin receptor antagonists are currently available for research use only. [Pg.210]

In the first phase of their research, Squibb tested a short-chain peptide isolated from the venom of the viper Bothrops jararaca, with which Vane was working in the laboratory, in human volunteers and showed that it did, indeed, inhibit the conversion of angiotensin I to angiotensin II after intravenous injection. The peptide was also shown to reduce blood pressure in patients when injected. Since the vast majority of peptides cannot be absorbed from the GI tract, Squibb scientists set out to prepare a nonpeptide compound that could be used orally and manufactured at acceptable cost. The design of a true peptidomimetic that became orally active had not been accomplished at that time. Squibb then carried out... [Pg.12]

Researchers have reasoned that if the water-soluble peptide leu-enkephalin could be conjugated with an oxidizable hydrophobic chain, and further shielded with a hydrophobic domain provided by cholesterol via an ester linkage, the modihed leu-enkephalin could become sufficiently hydrophobic to breach the blood-brain barrier. The oxidation of one of the engineered domains in the brain would produce an ionic form that cannot redistribute back into blood, and is essentially locked in. The ester linkages could then be hydrolyzed by esterases in brain tissues to release biologically active leu-enkephalin (Figure 13.12). [Pg.362]

We wish to thank our former colleagues at the Institut fiir Peptidforschung (now IPF Pharmaceuticals), Prof. Dr. Dr. Wolf-Georg Forssmann for his pioneering work in comprehensive peptide analysis from blood and Dr. Manfred Raida (present address Cellzome AG) for his invaluable work in analytical peptide chemistry. This work was supported in part by grants from the German Ministry for Education and Research, BMBF (FKZ 0312815), and the Lower Saxony Ministry for Economy and Technology (203.19-32329-5-354). [Pg.130]


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See also in sourсe #XX -- [ Pg.118 ]




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