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- W101777779 abstract "This chapter discusses the synthesis and activity of angiotensin analogues—mostly heptapeptides—in which the arginine moiety is replaced by similar residues of varied structure and configuration. The structure of the natural octapeptide is Asp-Arg-Val-Tyr-Ile-His-Pro-Phe. The heptapeptide obtained by omitting the first amino-acid residue is considerably active. However, the hexapeptide differing from the heptapeptide by lack of the basic arginine molecule has a strongly reduced activity. The positive charge at the end of the chain of the arginine residue of the heptapeptide plays a role in the binding of the molecule onto a certain receptor or in catalyzing a certain reaction. Factors, such as length and flexibility of the chain bearing the positive charge, can determine the ease and probability for the charged grouping to occupy the right position. Besides the guanidinium or ammonium group at the end of the side-chain, there is also present an α-NH3 group in the peptides. For good activity, the two positive charged groups must each occupy a definite position. This can be easily achieved with a terminal D-amino-acid residue than with its mirror image." @default.
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- W101777779 date "1966-01-01" @default.
- W101777779 modified "2023-09-27" @default.
- W101777779 title "SYNTHESIS AND ACTIVITY OF ANGIOTENSIN ANALOGUES (MOSTLY HEPTAPEPTIDES) IN WHICH THE ARGININE MOIETY IS REPLACED BY SIMILAR RESIDUES OF VARIED STRUCTURE AND CONFIGURATION" @default.
- W101777779 cites W1988085627 @default.
- W101777779 doi "https://doi.org/10.1016/b978-1-4831-9851-4.50041-3" @default.
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