Peptides biological function

Mangoni, M. L., Papo, N., Mignogna, G., et al. (2003) Ranacyclins, a new family of short cyclic antimicrobial peptides biological function, mode of action, and parameters involved in target specificity. Biochemistry, 42, 14023-14035. 

A dipeptide is a molecule consisting of two ammo acids joined by a peptide bond A tnpeptide has three ammo acids joined by two peptide bonds a tetrapeptide has four ammo acids and so on Peptides with more than 30-50 ammo acids are polypeptides Proteins are polypeptides that have some biological function... 

Biological function and chemistry of endothelin, vasoactive peptide with macro-cyclic fragments formed by disulfide bridges between cysteine residues 99CCC1211. 

The neuropeptide Y (NPY) belongs to a family of peptides that includes peptide YY and pancreatic polypeptide, and it is associated with several diseases such as asthma, immune system disorders, inflammatory diseases, anxiety, depression and diabetes mellitus. NPY is found in the central and peripheral nervous system, and its biological functions are mediated by interactions with five receptor sub-types, i.e. Yl, Y2, Y4, Y5 and Y6. Several studies indicate that the feeding behavior is influenced by interactions between NPY and Yl and Y5. Deswal and Roy used Cerius descriptors and genetic function approximation QSAR to investigate the structural determinants for the inhibition potency of 24 compounds with the general structure 4 for the NPY Y5 receptor [31]. The best QSAR (H = 0.720,... 

Abstract To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR, which makes use of macroscopically oriented lipid bilayers to study selectively isotope-labelled peptides. Native biomembranes, however, have a far more complex lipid composition and a significant non-lipidic content (protein and carbohydrate). Model membranes, therefore, are not really adequate to address questions concerning for example the selectivity of these membranolytic peptides against prokaryotic vs eukaryotic cells, their varying activities against different bacterial strains, or other related biological issues. 

The sequence of amino acids in a polypeptide chain is known as the primary structure. This feature is genetically determined and is responsible not only for the final shape of the protein but also for its physical characteristics and, ultimately, for its biological function. Proteins are made up of about 22 amino acids, which are linked by the peptide bond (Figure 11.1), an amide linkage involving the amino group of one amind acid and the carboxyl group of another. 

Oxytocin, a peptide which initiates uterine contractions during labour is identical in structure to ADH except at position 8 where a leucine residue replaces arginine. The close structural similarity but radically different biological functions, illustrate how specific some hormone receptors are in recognising only their own signal . 

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