[9-Aminoacetone]oxytocin and [8-p-aminobenzamide, 9-des-glycinamide]oxytocin: Chemical synthesis and properties

1982 ◽  
Vol 47 (1) ◽  
pp. 338-348 ◽  
Author(s):  
Jan Hlaváček ◽  
Ivo Frič ◽  
Tomislav Barth ◽  
Karel Jošt
Keyword(s):  
Chemical Synthesis ◽  
Structural Changes ◽  
Biological Activities ◽  
Cd Spectra ◽  
Terminal Part ◽  
Amino Terminal ◽  
Carboxy Terminal ◽  
Cyclic Part

[9-Aminoacetone]oxytocin and [8-p-aminobenzamide, 9-des-glycinamide]oxytocin were prepared by condensation of amino-terminal linear hexapeptide with peptides simulating the carboxy-terminal tripeptide chain of oxytocin, according to the 6 + 3 scheme. Both the analogues had significantly lower biological activities than oxytocin. CD spectra of the analogues were compared with those of oxytocin and [9-des-glycine]oxytocin in order to study the effect of structural changes in the carboxy-terminal part of the analogues on the conformation of their cyclic part.

scholarly journals The Drosophila Gene for Antizyme Requires Ribosomal Frameshifting for Expression and Contains an Intronic Gene for snRNP Sm D3 on the Opposite Strand

1998 ◽  
Vol 18 (3) ◽  
pp. 1553-1561 ◽  
Author(s):  
Ivaylo P. Ivanov ◽  
Karl Simin ◽  
Anthea Letsou ◽  
John F. Atkins ◽  
Raymond F. Gesteland
Keyword(s):  
Open Reading Frame ◽  
P Element ◽  
Terminal Part ◽  
Ribosomal Frameshifting ◽  
Reading Frame ◽  
Muscle Cell Differentiation ◽  
Amino Terminal ◽  
Opposite Strand ◽  
Carboxy Terminal ◽  
Transposon Insertions

ABSTRACT Previously, a Drosophila melanogaster sequence with high homology to the sequence for mammalian antizyme (ornithine decarboxylase antizyme) was reported. The present study shows that homology of this coding sequence to its mammalian antizyme counterpart also extends to a 5′ open reading frame (ORF) which encodes the amino-terminal part of antizyme and overlaps the +1 frame (ORF2) that encodes the carboxy-terminal three-quarters of the protein. Ribosomes shift frame from the 5′ ORF to ORF2 with an efficiency regulated by polyamines. At least in mammals, this is part of an autoregulatory circuit. The shift site and 23 of 25 of the flanking nucleotides which are likely important for efficient frameshifting are identical to their mammalian homologs. In the reverse orientation, within one of the introns of the Drosophila antizyme gene, the gene for snRNP Sm D3 is located. Previously, it was shown that two closely linked P-element transposon insertions caused the gutfeelingphenotype of embryonic lethality and aberrant neuronal and muscle cell differentiation. The present work shows that defects in either snRNP Sm D3 or antizyme, or both, are likely causes of the phenotype.

scholarly journals Significance of the intact polypeptide chains of human fibrinogen in ADP-induced platelet aggregation

Blood ◽  
1977 ◽  
Vol 49 (4) ◽  
pp. 635-644
Author(s):  
S Niewiarowski ◽  
AZ Budzynski ◽  
B Lipinski
Keyword(s):  
Platelet Aggregation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Human Platelets ◽  
Terminal Part ◽  
Human Fibrinogen ◽  
Amino Terminal ◽  
Carboxy Terminal ◽  
Stage 1 ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

The presence of human fibrinogen in suspensions of washed human platelets is a requirement for ADP-induced platelet aggregation. Digestion of fibrinogen with plasmin destroys this function of the protein. The high solubility fraction of Kabi fibrinogen, fragment X (stage 1) and framgent X (stage 2), are two, eight, and ten times, respectively, less potent in promoting ADP-induced platelet aggregation, as compared with intact fibrinogen. Fragments Y and D and the mixture of reduced and carboxymethylated chains of human fibrinogen do not support ADP-induced platelet aggregation at all. SDS polyacrylamide gel electrophoresis of nonreduced and reduced fibrinogen and its derivatives indicates that the intact fibrinogen molecule is essential for ADP-induced platelet aggregation. It is suggested that the carboxy-terminal part of the Aalpha chain and possibly also the amino-terminal part of the Bbeta chain are required for the platelet aggregation-promoting function of fibrinogen.

[7-Glycine]deamino-1-carba-vasopressin: Synthesis and pharmacological properties

1981 ◽  
Vol 46 (1) ◽  
pp. 278-285 ◽  
Author(s):  
František Brtník ◽  
Tomislav Barth ◽  
Karel Jošt
Keyword(s):  
Substantial Decrease ◽  
Pharmacological Properties ◽  
Amino Terminal ◽  
Glycine Derivative ◽  
Carboxy Terminal ◽  
Cyclic Part ◽  
Vasopressin Synthesis

[8-Arginine]deamino-1-carba-vasopressin and its 7-glycine derivative were prepared by condensation of the amino-terminal, cyclic part of the molecule with carboxy-terminal tripeptide amides. Replacement of proline by glycine in the position 7 results in a substantial decrease in the vasopressin-like activities, the oxytocin-like activities remaining unchanged.

scholarly journals Significance of the intact polypeptide chains of human fibrinogen in ADP-induced platelet aggregation

Blood ◽  
1977 ◽  
Vol 49 (4) ◽  
pp. 635-644 ◽  
Author(s):  
S Niewiarowski ◽  
AZ Budzynski ◽  
B Lipinski
Keyword(s):  
Platelet Aggregation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Human Platelets ◽  
Terminal Part ◽  
Human Fibrinogen ◽  
Amino Terminal ◽  
Carboxy Terminal ◽  
Stage 1 ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

Abstract The presence of human fibrinogen in suspensions of washed human platelets is a requirement for ADP-induced platelet aggregation. Digestion of fibrinogen with plasmin destroys this function of the protein. The high solubility fraction of Kabi fibrinogen, fragment X (stage 1) and framgent X (stage 2), are two, eight, and ten times, respectively, less potent in promoting ADP-induced platelet aggregation, as compared with intact fibrinogen. Fragments Y and D and the mixture of reduced and carboxymethylated chains of human fibrinogen do not support ADP-induced platelet aggregation at all. SDS polyacrylamide gel electrophoresis of nonreduced and reduced fibrinogen and its derivatives indicates that the intact fibrinogen molecule is essential for ADP-induced platelet aggregation. It is suggested that the carboxy-terminal part of the Aalpha chain and possibly also the amino-terminal part of the Bbeta chain are required for the platelet aggregation-promoting function of fibrinogen.

scholarly journals Advantage of a baculovirus expression system for protein-protein interaction studies. Involvement of posttranslational phosphorylation in the interaction between wt p53 protein and poly(ADP-ribose) polymerase-1.

2005 ◽  
Vol 52 (3) ◽  
pp. 713-719 ◽  
Author(s):  
Gerald Schmid ◽  
Jacek Wojciechowski ◽  
Józefa Wesierska-Gadek
Keyword(s):  
Complex Formation ◽  
Protein Interaction ◽  
P53 Protein ◽  
Full Length ◽  
Functional Domain ◽  
Terminal Part ◽  
Protein Protein Interaction ◽  
Amino Terminal ◽  
Carboxy Terminal ◽  
Parp 1

We recently observed an interaction between poly(ADP-ribose) polymerase-1 (PARP-1) and the tumor suppressor p53 protein. However, more extensive studies on both proteins, especially those on characterization of their domains involved in the interaction were difficult due to very low expression levels of p53 in mammalian cells. Therefore, we generated recombinant proteins for such studies. To clarify which domains of human PARP-1 and of human wild-type (wt) p53 were involved in this protein-protein interaction, we generated baculoviral constructs encoding full length or distinct functional domains of both proteins. Full length PARP-1 was simultaneously coexpressed in insect cells with full length wt p53 protein or its distinct truncated fragments and vice versa. Reciprocal immunoprecipitation of Sf9 cell lysates revealed that the central and carboxy-terminal fragments of p53 each were sufficient to confer binding to PARP-1, whereas the amino-terminal part harbouring the transactivation functional domain was dispensable. On the other hand, the amino-terminal and central fragments of PARP-1 were both necessary for complex formation with p53 protein. Since the most important features of p53 protein are regulated by phosphorylation, we addressed the question whether its phosphorylation is essential for the binding between the two proteins. Baculovirally expressed wt p53 was post-translationally modified. At least six distinct p53 isomers were resolved by immunoblotting following two-dimensional separation of baculovirally expressed wt p53 protein. Using specific phospho-serine antibodies, we identified phosphorylation of baculovirally expressed p53 protein at five distinct sites. To define the role of p53 phosphorylation, pull-down assays using untreated and dephosphorylated p53 protein were performed. Dephosphorylated p53 failed to bind PARP-1, indicating that complex formation between the two proteins was regulated by phosphorylation of p53. The marked phosphorylation of p53 at Ser392 observed in unstressed cells suggests that the phosphorylated carboxy-terminal part of p53 undergoes complex formation with PARP-1 resulting in masking of the NES and thereby preventing its export.

Advances in Synthesis and Medicinal Applications of Compounds Derived from Phthalimide

2020 ◽  
Vol 17 (4) ◽  
pp. 252-270
Author(s):  
Marcel L. Almeida ◽  
Maria C.V.A. Oliveira ◽  
Ivan R. Pitta ◽  
Marina G.R. Pitta
Keyword(s):  
Chemical Synthesis ◽  
Biological Activities ◽  
Sedative Effects ◽  
Phthalimide Derivative ◽  
Anti Inflammatory

Phthalimide derivatives have been presenting several promising biological activities in the literature, such as anti-inflammatory, analgesic, antitumor, antimicrobial and anticonvulsant. The most well-known and studied phthalimide derivative (isoindoline-1,3-dione) is thalidomide: this compound initially presented important sedative effects, but it is now known that thalidomide has effectiveness against a wide variety of diseases, including inflammation and cancer. This review approaches some of the recent and efficient chemical synthesis pathways to obtain phthalimide analogues and also presents a summary of the main biological activities of these derivatives found in the literature. Therefore, this review describes the chemical and therapeutic aspects of phthalimide derivatives.

A Mini Review on the Chemical Synthesis of Resveratrol

2020 ◽  
Vol 17 (5) ◽  
pp. 546-558
Author(s):  
Hong Huang ◽  
Ruonan Liu ◽  
Wenhua Ou
Keyword(s):  
Cardiovascular Disease ◽  
Chemical Synthesis ◽  
Neurodegenerative Diseases ◽  
Biological Activities ◽  
Polyphenolic Compound ◽  
Chemical Methods

Resveratrol is a polyphenolic compound and has been shown to possess numerous biological activities, which could possibly be applied to the prevention and/or treatment of cancer, cardiovascular disease, and neurodegenerative diseases. This review summarizes the progress of different chemical methods in the preparation of resveratrol.

Preparation, spectral properties and biological activities of 5-bromo-6-methyl-2'-deoxyuridine and 5-iodo-6-methyl-2'-deoxyuridine

1980 ◽  
Vol 45 (8) ◽  
pp. 2364-2370 ◽  
Author(s):  
Antonín Holý ◽  
Erik De Clercq
Keyword(s):  
Antiviral Activity ◽  
Spectral Properties ◽  
De Novo ◽  
Biological Activities ◽  
Rabbit Kidney ◽  
Kidney Cells ◽  
Cd Spectra ◽  
Methyl Derivatives ◽  
Primary Rabbit

Reaction of 3',5'-di-O-benzoyl-6-methyl-2'-deoxyuridine (IIa) with elementary bromine or iodine afforded 5-halogeno derivatives IIc and IId which on methanolysis gave 5-bromo-6-methyl-2'-deoxyurine (Ic) and 5-iodo-6-methyl-2'-deoxyurine (Id), respectively. The CD spectra of Ic, Id and 6-methyl-2'-deoxyuridine (Ia) are compared and discussed with regard to determination of the nucleoside conformation. Unlike 5-bromo- and 5-iodo-2'-deoxyuridine, the 6-methyl derivatives Ic and Id exhibit neither antibacterial nor antiviral activity. Nor do they exert any antimetabolic effect on the de novo DNA synthesis in primary rabbit kidney cells.

Synthesis and biological properties of cholecystokinin heptapeptide analogues containing D- and L-forms of tert-leucine or neopentylglycine in position 5

1991 ◽  
Vol 56 (10) ◽  
pp. 2209-2217 ◽  
Author(s):  
Jan Hlaváček ◽  
Jana Pírková ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Lenka Maletínská
Keyword(s):  
Gall Bladder ◽  
Solid Phase ◽  
Biological Activities ◽  
Biological Properties ◽  
Phase Synthesis ◽  
Structural Modifications ◽  
Bladder Contraction ◽  
Anorectic Effect ◽  
Carboxy Terminal ◽  
Anorectic Activity

Using solution or solid-phase synthesis we prepared the cholecystokinin fragment Boc-CCK-7 (Boc-Tyr-(SO3-.Na+)-Met-Gly-Trp-Met-Asp-PheNH2) and its four analogues in which the methionine moiety (Met) in the carboxy-terminal part is replaced by tert-leucine (Tle) or neopentylglycine (Neo) residue or D-enantiomers of these non-coded amino acids. These structural modifications led to reduction of the studied biological activities (gall bladder contraction, anorectic activity, analgetic and sedation activity) of all prepared analogues except Boc[Neo5]-CCK-7 which, being less analgetically active, retains full gall bladder and sedation activity of CCK-8. Moreover, its anorectic activity is substantially higher (400%). This analogue is very interesting particularly for its selectively increased (4x) anorectic effect compared with that of CCK-8.

Interaction Between Mutations in the suppressor of Hairy wing and modifier of mdg4 Genes of Drosophila melunogaster Affecting the Phenotype of gypsy-Induced Mutations

Genetics ◽  
1996 ◽  
Vol 142 (2) ◽  
pp. 425-436 ◽  
Author(s):  
Pavel Georgiev ◽  
Marina Kozycina
Keyword(s):  
Mutagenic Effect ◽  
Induced Mutations ◽  
Binding Region ◽  
Direct Inhibition ◽  
Amino Terminal ◽  
Acidic Domain ◽  
Complete Inactivation ◽  
Insulation Effect ◽  
Gypsy Retrotransposon ◽  
Carboxy Terminal

Abstract The suppressor of Hairy-wing [su(Hw)] protein mediates the mutagenic effect of the gypsy retrotransposon by repressing the function of transcriptional enhancers located distally from the promoter with respect to the position of the su(Hw)-binding region. Mutations in a second gene, modifier of mdg4, also affect the gypsy-induced phenotype. Two major effects of the mod(mdg4)lul mutation can be distinguished: the interference with insulation by the su(Hw)-binding region and direct inhibition of gene expression that is not dependent on the su(Hw)-binding region position. The mod(mdg4)lul mutation partially suppresses ct6, scD1 and Hw1 mutations, possibly by interfering with the insulation effect of the su(Hw)-binding region. An example of the second effect of mod(mdg4)lul is a complete inactivation of yellow expression in combination with the y  2 allele. Phenotypic analyses of flies with combinations of mod(mdg4)lul and different su(Hw) mutations, or with constructions carrying deletions of the acidic domains of the su(Hw) protein, suggest that the carboxy-terminal acidic domain is important for direct inhibition of yellow transcription in bristles, while the amino-terminal acidic domain is more essential for insulation.

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