[Regulation of adenylyl cyclase activity in the @entity35 testes by acylated derivatives of peptide 562-572 of XXXX ].

@entity1 @entity844 @entity2365 @entity19658 @entity7813 @entity71801 @entity35 @entity15409
One of directions of the search of hormonal signaling systems regulators is the development of peptides that correspond to the cytoplasmic regions of @entity71801 ( @entity71801 ). Modification of the pepti- des with hydrophobic radicals increases their efficiency and selectivity. But currently is not studied as the acti- vity of the peptide depends on the localization of the hydrophobic radicals, their number and the chemical natu- re. The aim of this work was the synthesis of modified by @entity844 radicals derivatives of peptide 562-572 corresponding to the C-terminal region of @entity7813 ( @entity7813 ), and the study of regulatory ef- fects of the acylated @entity7813 -peptides on the basal and hormone-stimulated activity of adenylyl cyclase (AC) in the @entity35 tissues. To elucidate the effect of localization of hydrophobic radicals and their number the modification of peptide 562-572 only at the N- or C-terminus or at both ends was carried out. To study the effect of hydrop- hobicity the residues ofpalmitic ( @entity15409 ) and decanoic (Dec) acids were selected. Using a solid phase strategy we have synthesized unmodified peptide NDTKIAKK-Nle-A562-572-KA (1) and five of its acylated analogues, such as N[K(Dec)]DTKIAKK-Nle-A562-572-KA (2), NKDTKIAKK-Nle-A562-572-[K(Dec)]A (3), N[K(Dec)] DTKIAKK-Nle-A562-572-[K(Dec)]A (4), N[K( @entity15409 )]DTKIAKK-Nle-A562-572-KA (5), and NKDTKIAKK-Nle- A562--572-[K( @entity15409 )]A (6). Peptide 6 modified with @entity2365 at the C-terminus to a large extent increased the ba- sal AC activity and reduced AC stimulating effect of @entity1 chorionic gonadotropin (hCG) in the testes of @entity35 , peptides 3 and 4 modified with @entity19658 at the C-terminus were less effective, but exceeded in activity the un- modified peptide 1, while peptides 2 and 5 acylated at the N-terminus were little active. The action of peptides was characterized by the tissue and the receptor specificity. Thus, the modification of @entity7813 -peptide 562-572 with @entity844 radicals at the C-terminus increases its regulatory effect on the functional activity of the adenyla- te cyclase system in the @entity35 testes, indicating promising the modification of @entity71801 -peptides with hydrophobic radicals. These data support the hypothesis that the hydrophobic radical to be localized in the locus of @entity71801 -peptide, where a transmembrane domain is located in the receptor.
