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Wyszukujesz frazę "insect peptide" wg kryterium: Temat


Wyświetlanie 1-7 z 7
Tytuł:
Biological evaluation of analogues of an insect neuropeptide proctolin.
Autorzy:
Woźnica, Iwona
Szeszel-Fedorowicz, Wioletta
Rosiński, Grzegorz
Konopińska, Danuta
Powiązania:
https://bibliotekanauki.pl/articles/1043325.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
proctolin analogues
proctolin
insect myotropic peptide proctolin
Opis:
Continuing our studies on proctolin (Arg-Tyr-Leu-Pro-Thr) we performed the synthesis and biological evaluation of 52 analogues substituted in position 2, 3, 4, and 5 of the peptide chain. The peptides were bioassayed for cardiotropic activity in vitro on Tenebrio molitor and myotropic activity on foregut of Schistocerca gregaria. Twenty analogues retained 20-80% of proctolin activity.
Źródło:
Acta Biochimica Polonica; 2004, 51, 1; 115-119
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The search for new biological activities for selected insect peptides
Autorzy:
Kuczer, M.
Dziubasik, K.
Luczak, M.
Majewska, A.
Kamysz, W.
Saniewska, A.
Konopinska, D.
Powiązania:
https://bibliotekanauki.pl/articles/55140.pdf
Data publikacji:
2008
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
antitumour peptide
antifungal activity
antiviral peptide
oostatic peptide
antiviral activity
Phoma narcissi
Botrytis tulipae
colony growth
biological property
antimicrobial activity
insect peptide
biological activity
insect
peptide
Opis:
New biological properties of selected insect peptides are presented. The subjects of the investigation included insect oostatic peptides, like Neb-colloostatin (I) and Neb-TMOF(II), and/or insect peptides with antiviral or antitumor activity, such as alloferon (III) and its analogues modified at position 1 of the peptide chain. In the study was also included the oligopeptide Any-GS (VII) and its truncated analogues. The peptides were tested for antimicrobial activity on a series of bacterial species, antiviral activity against Human Herpes Virus type 1 (HHV-1) in vitro using a Vero cell line, and the growth and development of plant pathogens Phoma narcissi and Botrytis tulipae. The results of the biological investigations indicate that among the peptides investigated, compounds VII and IX inhibit the growth of plant pathogens P. narcissi and B. tulipae, whereas compounds I and II stimulate the mycelium growth of the aforementioned pathogens. Other peptides show slow antimicrobial activity but do not inhibit the replication of HHV-1 in Vero cells.
Źródło:
Pestycydy; 2008, 1-2; 5-11
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Antibacterial peptides of the moth Galleria mellonella
Autorzy:
Mak, Paweł
Chmiel, Dorota
Gacek, Grzegorz
Powiązania:
https://bibliotekanauki.pl/articles/1044082.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
antibacterial peptide
bacteriocin
insect immunity
hemolymph
cecropin
Opis:
The work describes purification and biochemical characterization of two inducible antimicrobial peptides from the hemolymph of Galleria mellonella. The peptides were isolated by a sequence of reversed-phase chromatography steps from the hemolymph of larvae immunized with viable bacteria. The first peptide is a member of the cecropin family while the second one is rich in proline residues and has a unique sequence.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 1191-1195
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Antinociceptive effect of MAS MT in rats
Autorzy:
Rykaczewska-Czerwinska, M.
Radosz, A.
Szymanowska-Dziubasik, K.
Konopinska, D.
Plech, A.
Powiązania:
https://bibliotekanauki.pl/articles/55342.pdf
Data publikacji:
2008
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
Tenebrio molitor
antinociceptive effect
rat
larva
brain
neuropeptide
insect neuropeptide
Manduca sexta
proctolin
myotropin
biological activity
peptide chain
peptide
Opis:
MAS MT is a myotropic decapeptide isolated from Manduca sexta. This peptide exerts stimulatory effect on insects heart-beat frequency. The present study was undertaken in order to determine a probable antinociceptive effect in rats of native synthetic decapeptide, MAS MT-I and its two analogs, heptapeptides MAS MT-II and MAS MT-III. All these peptides were applied directly into the lateral brain ventricle (icv) at three doses: 10, 25 and 50 nmol. The analgesic (antinociceptive) effect was evaluated by a tail immersion test. It was found that two doses of MAS MT-I: 25 and 50 nmol induced significant antinociceptive effect, while MAS MT-II and MAS MT-III exert a less antinociceptive effect in comparison with native MAS MT-I. Prior icv administration of naloxone, an opioid antagonist weakly blocked MAS MT-I effect. We conclude that antinociceptive effect of MAS MT-I in rats is not mediated by central opioid system.
Źródło:
Pestycydy; 2008, 3-4; 139-146
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Stereochemistry of insect kinin tetrazole analogues and their diuretic activity in crickets.
Autorzy:
Nachman, Ronald
Coast, Geoffrey
Kaczmarek, Krzysztof
Williams, Howard
Zabrocki, Janusz
Powiązania:
https://bibliotekanauki.pl/articles/1043327.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
constrained insect kinin analogue
tetrazole
diuresis
cis-peptide bond
β-turn mimetic
Opis:
Insect kinin analogues of the sequence Phe-Phe-ψ[CN4]-Ala-Trp-Gly-NH2 containing (L-Phe2,L-Ala3) and (L-Phe2,D-Ala3) stereochemical variants of the tetrazole moiety, a mimic of the type VI β-turn, demonstrate significant agonist and partial antagonist activity, respectively, in a cricket diuretic bioassay. A comparison of the solution conformations of these two stereochemical variants indicates a structural basis for their divergent bioactivities. The (D-Phe2,D-Ala3) stereochemical variant was synthesized and found to demonstrate significant agonist activity. The results further define stereochemical requirements for the diuretic activity of insect kinins in crickets and provide valuable information for the design of biostable analogues capable of disrupting digestive and diuretic processes in pest insects.
Źródło:
Acta Biochimica Polonica; 2004, 51, 1; 121-127
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effects of arginine substitutions on the cardioinhibitory activity of the Led-NPF-I neuropeptide
Autorzy:
Marciniak, P.
Slocinska, M.
Bednarz, P.
Grodecki, S.
Konopinska, D.
Rosinski, G.
Powiązania:
https://bibliotekanauki.pl/articles/55015.pdf
Data publikacji:
2009
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
cardioinhibitory activity
arginine substitution
mealworm beetle
Zophobas atratus
giant mealworm beetle
Led-NPF-I-peptide
insect
beetle
neuropeptide
Opis:
Effects of structural changes on the cardioinhibitory activity of the Led-NPF-I peptide (Ala-Arg-Gly-Pro-Gln-Leu-Arg-Leu-Arg-Phe-amide) were examined by replacing Arg residues in positions 2, 7 and 9. Replacement of L-Arg2 with another basic amino acid, such as Lys, His or D-Arg, did not abolish but rather promoted cardioinhibitory activity in giant mealworm beetle Zophobas atratus Fab. Agonistic peptides were also obtained by substitution of Arg residue in position 7 with Lys or D-Arg, and Arg in position 9 with His or D-Arg, respectively. All these analogues showed stronger cardioinhibitory effects than the native peptide at low concentration (10-9 M), and [Lys7]-, [D-Arg7]- and [D-Arg9]-Led-NPF-I also at the higher concentration (10-6 M). However, substitutions of the Arg residues in position 7 with His or in position 9 with Lys caused a loss of the cardioinhibitory activity. In addition, the replacement of Arg residues in all three positions with Lys or Orn caused a reduction of cardioinhibitory activity, although a single substitution of Arg in positions 2 or 7 with Lys yielded agonistic peptides. We conclude that the Arg2 position in the N-terminal region is more tolerant to structural modification than the other two Arg positions located in the C-terminal region.
Źródło:
Pestycydy; 2009, 1-4; 71-78
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
trans-Pro isosteres in the development of non-selective and selective mimetic agonists of insect pyrokinin neuropeptides: A review
Autorzy:
Nachman, R.J.
Powiązania:
https://bibliotekanauki.pl/articles/55206.pdf
Data publikacji:
2009
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
diapause hormone
physiological process
melanization
pupariation
pheromonotropin
neuropeptide
pyrokinin family
pheromone
diapause break
pheromone biosynthesis activating neuropeptide
insect
reddish colouration hormone
peptide
Opis:
The pyrokinin (PK) family plays a multifunctional role in an array of important physiological processes in a variety of insects. A PK active core analog containing an (E)-alkene, transPro isosteric component was evaluated in five disparate PK bioassays and/or in a recombinant PK receptor cell line, representing six different insect species. The assays included pheromone biosynthesis in the moth Heliothis peltigera, melanization in the larval Spodoptera littoralis, pupariation acceleration in the larval fly Neobellieria bullata, diapause termination in the moth Heliothis zea, and hindgut contraction in the cockroach Leucophaea maderae. This constrained analog demonstrated unselective agonist activity that approached, matched, or exceeded the activity of parent PK peptides of equal length in all six PK assays. The results provide strong evidence for the orientation of Pro and the core conformation adopted by PK neuropeptides during interaction with disparate PK receptors. A PK active core analog incorporating a second transPro motif, the dihydroimidazoline moiety, was found to demonstrate pure, selective agonism in the melanotropic bioassay, with no significant activity in three other PK bioassays. Both types of transPro isosteric analogs feature modification adjacent to the primary tissue-bound peptidase hydrolysis site that is expected to enhance biostability over natural PK peptides. The research further identifies two novel scaffolds with which to design either selective or non-selective mimetic PK analogs as potential leads in the development of environmentally favorable pest management agents capable of disrupting PK-regulated systems.
Źródło:
Pestycydy; 2009, 1-4; 33-39
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-7 z 7

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