Wyniki wyszukiwania - Biblioteka Nauki

1

Uklad opioidowy a odpornosc wrodzona - badania porownawcze. 1. Opioidy i receptory opioidowe

100%

Chadzinska M.

Postępy Biologii Komórki

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2007

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tom 34

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nr 2

251-262

2

Apoptoza ludzkich neutrofilow in vitro - wplyw egzogennych peptydow opioidowych.

100%

Sulowska Z. , Krawczyk K. , Tchorzewski H.

Działalność Naukowa PAN. Wybrane Zagadnienia

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2001

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tom 12

63-65

3

Rola peptydow opioidowych w zachowaniu sie zwierzat

100%

Panocka I.

Prace i Materiały Zootechniczne. Zeszyt Specjalny

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1992

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nr 01

41-48

4

Receptory opioidowe i ich selektywne ligandy peptydowe

100%

Piestrzeniewicz M. K. , Michna J. , Janecka A.

Postępy Biochemii

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2006

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tom 52

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nr 3

313-319

5

Rola greliny w modulowaniu proliferacji limfocytow u jagniat

84%

Zubel J. , Pierzchala-Koziec K.

Folia Universitatis Agriculturae Stetinensis. Zootechnica

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2006

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tom 48

37-43

6

Rola peptydów opioidowych w ośrodkowej modulacji zachowania pokarmowego u owiec

84%

Wielgosz M. , Kania B. F.

Życie Weterynaryjne

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2014

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tom 89

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nr 02

7

Endogenne peptydy opioidowe: nowe cytokiny?

84%

Pasnik J.

Postępy Biologii Komórki

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1997

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tom 24

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nr 4

519-542

8

Biwalentne ligandy receptorów opioidowych

67%

Frączak O. , Olma A.

Wiadomości Chemiczne

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2014

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tom [Z] 68, 3-4

233--255

EN

Opioids are the oldest drugs know to humanity, which have been and continue to be used for the treatment of chronic pain. Unfortunately they have a large numbers of side effects [1–6]. Three main types of opioid receptors μ (MOR), δ (DOR) and κ (KOR) are known [8]. The ORL1 receptor was classified as the fourth member of opioid receptor family [9]. Opioid receptors can form homodimers and the following heterodimers: DOR-KOR, DOR-MOR and KOR-MOR [13c,d,f, 14]. Specially designed ligands which are able to penetrate the BBB are used to study physiological consequences of opioid receptor homo- and heterodimerization, and as new analgesics. Bivalent ligands are defined as compounds that contain two pharmacophoric units, an appropriately designed spacer to separate and define the two pharmacophores, and a linker unit to connect the pharmacophores, to the spacer (Fig. 1) [16]. The affinity of a ligand to its target depends on its fundamental kinetic association and dissociation rate constants (Scheme 1) [24]. Bivalent ligands interacting with the opioid receptors have been divided into three groups: nonpeptide, peptide- nonpeptide and peptide homo- or heterodimers. Nonpeptide bivalent ligands (4–21, 27–41 and 44–45) containing different pharmacophores (selective opioid agonists or/and antagonists) connected with designed linkers have potent analgesic properties [25–34]. Compound 35 may be useful in the treatment of opioid dependence. Studies of peptide-nonpeptide ligands, which are a combination of “address” segments of endogenous opioid peptides and selective alkaloid ligand (47–50) indicate that peptide part of the analogues can modulate the receptor selectivity of the attached alkaloid pharmacophores [35]. Series of peptide-nonpeptide ligands containing different classes of opioid peptides and fentanyl (52–86) were synthesized and tested for binding affinity to μ and δ opioid receptors [38–40]. Good opioid affinity and antinociceptive activity of some of the obtained bivalent ligands (57, 61, 63) suggesting that a novel class of analgesics can be further developed utilizing this approach. Among homobivalent ligands the most important is biphalin 87 and its analogues (88–124) [41–53]. Analgesic potency of the most active ligand 112 is greater than parent peptide (biphalin) and morphine.

9

Biologicznie aktywne peptydy z bialek mleka

67%

Stepaniak L.

Przemysł Spożywczy

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1996

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tom 50

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nr 04

17-18

PL

Odkrycie biologicznie aktywnych peptydów w hydrolizatach białek żywności rozszerza pojęcie terminu wartości odżywczej. Kazeina i białka serwatkowe mleka kobiecego i krowiego są szczególnie bogate w sekwencje aminokwasów, które mogą tworzyć peptydy o różnych biologicznych właściwościach. Białka te zawierają sekwencje peptydów, które wiążą i transportują metale, mają właściwości opioidowe oraz wpływają na procesy regulacji ciśnienia i krzepliwości krwi. Niektóre peptydy z białek mleka wpływają korzystnie na procesy trawienia i wykazują aktywność antymikrobiologiczną. ß-kazomorfina-7 (fragment 60-66 ß-kazeiny) poza właściwościami opioidowymi hamuje aktywność enzymu konwertującego angiotensynę, 70 kDa wewnątrzkomórkową endopeptydazę oraz 95 kDa wewnątrzkomórkową aminopeptydazę z Lactococcus. Peptydy stanowiące fragment 58-72 ß-kazeiny, który zawiera sekwencje ß-kazomorfiny oraz fragment 193-209 ß-kazeiny zidentyfikowano w serze; peptydy te hamowały również aktywność wymienionych enzymów Lactococcus. Wiele peptydów, stanowiących część sekwencji białek mleka, może znaleźć zastosowanie jako dietetyczne dodatki do żywności lub może być stosowanych w farmakologii. Wydają się uzasadnione również dalsze badania nad peptydami z białek mleka, które hamują aktywność proteaz, ważnych w dojrzewaniu sera oraz innych proteaz występujących w żywności.

EN

The discovery of biologically active peptides in hydrolysates from food proteins broaders the definition of nutritive value. Human and bovine caseins and whey proteins are especially rich in sequences of amino acids which can yield peptides having different biological activities. These proteins contain sequences forming peptides which bind and carry metals, which have opiate and immunomodulating activity, and which can influence regulation of blood clotting and blood pressure. Some peptides from milk proteins influence positively digestion of food and show antimicrobial activity, ß-casomorphin-7 ß-casein f 60-66) apart of opiate properties inhibited angiotensin converting enzyme, a 70 kDa intracellular endopeptidase and a 95 kDa intracellular endopeptidase from Lactococcus. ß-casein fragments 58-72 which contain structure of ß-casomorphin-7 and ß-casein f 193-209 were identified in cheese and found to be inhibitory against the two Lactococcus enzymes. Many peptides having partial sequences of milk proteins may find application as dietetic food additives or in pharmacology. Further research on peptides inhibitory to proteases important for ripening of cheeses and proteases occurring in other foods is also warranted.

10

Wplyw opioidow na steroidogeneze w komorkach ziarnistych i oslonki wewnetrznej pecherzykow jajnikowych swin; mechanizm dzialania agonisty opioidowego FK 33-824

67%

Kaminski T.

Postępy Biologii Komórki

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2005

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tom 32

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nr 3

477-493

11

Programowanie bezpiecznej i prozdrowotnej zywnosci

67%

Kostyra H. , Kujawska E. , Kostyra E.

Przegląd Mleczarski

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2002

|

nr 01

16-20

12

Badanie struktury i dynamiki N-terminalnych sekwencji dermorfiny i ich analogów z wykorzystaniem spektroskopii NMR w ciele stałym i rentgenografii

59%

Trzeciak-Karlikowska K.

Wiadomości Chemiczne

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2012

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tom [Z] 66, 9-10

867-891

EN

Deltorphin I (Tyr-d-Ala-Phe-Asp-Val-Val-Gly-NH_2) and dermorphin (Tyr-d-Ala-Phe- -Gly-Tyr-Pro-Ser-NH_2) are natural opioid peptides that have been isolated from the skin of South American frogs [1]. The presence of d-amino acid is crucial for their biological activity. The synthetic analogs of given heptapeptides containing l-alanine are not analgesics [2]. Analysis of the influence of stereochemistry on molecular packing, dynamics and biological functions of neuropeptides is still important for receptor studies and practical applications (e.g. design of new selective pain killers). Presented research is focused on the structure and dynamics of two N-terminal sequences of dermorphin: tripeptide Tyr-d-Ala-Phe 1, tetrapeptide Tyr-D-Ala-Phe-Gly 2, and their analogs with l-alanine: Tyr-Ala-Phe 3 and Tyr-Ala-Phe-Gly 4, using solid state NMR and X-ray diffraction. This study clearly demonstrates that 1 and 2 crystallized under different conditions to form exclusively one structure [3, 4]. In contrast, tripeptide and tetrapeptide with l-Ala in the sequence very easily form different crystal modifications. Tyr-Ala-Phe 3 crystallizes into two forms: 3a and 3b [5], while Tyr-Ala-Phe-Gly 4 gives three modifications: 4a, 4b and 4c [4]. It seems that one of the factors, which can be important in the preorganization mechanism anticipating the formation of crystals, is the intramolecular CH-đ interaction between aromatic rings of tyrosine and/or phenylalanine and the methyl group of alanine. Such interaction is possible only for d-Ala residue. For l-Ala in the peptide sequence, the methyl group is aligned on the opposite side with respect at least to one of the aromatic groups. It can be further speculated that such internal CH-π contacts can also occur during the interaction of ligand–receptor, making the message sequence of opioid peptides more rigid and finally selective. By employing different NMR experiments (e.g. PISEMA MAS and PILGRIM) it was proven that the main skeleton of analyzed peptides is rigid, whereas significant differences in the molecular motion of the aromatic residues were observed [4, 6]. Solid state 2H NMR spectroscopy of samples with deuterium labeled aromatic rings: Tyrd4-d-Ala-Phe 5, Tyr-d-Ala-Phed5 6, Tyrd4-Ala-Phe 7, Tyr-Ala-Phe^d5 8 was used to analyze the geometry and time scale of the molecular motion. At ambient temperature, the tyrosine ring of sample 5 is rigid and in the sample 6 the phenylalanine ring undergoes a "π -flip". The tyrosine rings of form I of 7 and 8 are static, while the phenylalanine rings of form II of 7 and 8 undergo a fast regime exchange [6]. Variable temperature 2H measurements proved that the tyrosine and phenylalanine rings of two forms of compounds 7 and 8 became more mobile with increasing temperature. In contrast, the aromatic rings of samples 5 and 6 preserve their dynamics regime (static tyrosine and "π -flip" phenylalanine) in a large range of temperatures [6]. The analysis of 13C, 15N labeled tetrapeptide Tyr-D-Ala-Phe-Gly 2’-phospholipid membrane interactions suggests that peptide 2’ is aligned on the surface of the membrane (RFDR MAS) and the sandwich-like π -CH_3-π arrangement of the pharmacophore is preserved (DARR) [7].

13

Bioaktywne skladniki bialkowej frakcji mleka

51%

Bernatowicz E. , Reklewska B.

Przegląd Hodowlany

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2003

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tom 71

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nr 03

1-10