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    Wyświetlanie 1-9 z 9
    Tytuł:
    Synthesis and binding properties of deltorphin I analogues containing (R) and (S)-α-hydroxymethylnaphtylalanine.
    Autorzy:
    Olma, Aleksandra
    Gniadzik, Agnieszka
    Lipkowski, Andrzej
    Łachwa, Magdalena
    Powiązania:
    https://bibliotekanauki.pl/articles/1044072.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    deltorphin I analogues
    amphiphilic amino acids
    α,α-disubstituted amino acids
    opioid peptides
    opioid receptor binding
    α-hydroksymethylamino acids
    Opis:
    New analogues of deltorphin I (DT I), in which the phenylalanine residue in position 3 is substituted with amphiphilic α,α-disubstituted amino acid enantiomers, (R) and (S)-α-hydroxymethylnaphtylalanine, were synthesized and tested for μ and δ opioid receptor affinity and selectivity. Although both analogues have lower affinity to δ receptors than DT I, they both expressed specificity to δreceptors.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 1165-1168
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Biased versus unbiased randomness in homo-polymers and copolymers of amino acids in the prebiotic world
    Autorzy:
    Mosqueira, Fernando
    Negron, Alicia
    Ramos, Sergio
    Polanco, Carlos
    Powiązania:
    https://bibliotekanauki.pl/articles/1039646.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    polarity of amino acids
    homo-peptides
    prebiotic co-polypeptides
    lysine
    Markov chain
    prebiotic homo polymerization of amino acids
    Opis:
    The polymerization of amino acids under anhydrous prebiotic conditions was first studied several decades ago. Here we use a stochastic model stressing the relevant role of the polarity of amino acids in the formation of oligopeptides in a prebiotic milieu. Our goal is to outline the predominance of co-polypeptides over homo-polypeptides, resulting not only from the randomness, but also from polarity properties of amino acids. Our results conclude that there was a higher probability of the formation of co-polypeptides than of homo-polymers. Besides, we may hypothesize that the former would have a more ample spectrum of possible chemical functions than homo-polypeptides.
    Źródło:
    Acta Biochimica Polonica; 2012, 59, 4; 543-547
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Computational model of abiogenic amino acid condensation to obtain a polar amino acid profile
    Autorzy:
    Polanco, Carlos
    Buhse, Thomas
    Samaniego, José
    Castañón González, Jorge
    Estrada, Miguel
    Powiązania:
    https://bibliotekanauki.pl/articles/1039283.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    amino acids
    proteinoids
    origins of life
    polarity
    computer simulations
    Opis:
    In accordance with the second law of thermodynamics, the Universe as a whole tends to higher entropy. However, the sequence of far-from-equilibrium events that led to the emergence of life on Earth could have imposed order and complexity during the course of chemical reactions in the so-called primordial soup of life. Hence, we may expect to find characteristic profiles or biases in the prebiotic product mixtures, as for instance among the first amino acids. Seeking to shed light on this hypothesis, we have designed a high performance computer program that simulates the spontaneous formation of the amino acid monomers in closed environments. The program was designed in reference to a prebiotic scenario proposed by Sydney W. Fox. The amino acid abundances and their polarities as the two principal biases were also taken into consideration. We regarded the computational model as exhaustive since 200 000 amino acid dimers were formed by simulation, subsequently expressed in a vector and compared with the corresponding amino acid dimers that were experimentally obtained by Fox. We found a very high similarity between the experimental results and our simulations.
    Źródło:
    Acta Biochimica Polonica; 2014, 61, 2; 253-258
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Prenyl sulfates as alkylating reagents for mercapto amino acids
    Autorzy:
    Maltsev, Sergey
    Sizova, Olga
    Utkina, Natalia
    Shibaev, Vladimir
    Chojnacki, Tadeusz
    Jankowski, Wieslaw
    Swiezewska, Ewa
    Powiązania:
    https://bibliotekanauki.pl/articles/1040690.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cysteamine
    geraniol
    cysteine
    S-prenylation
    nerol
    lipidated amino acids
    Opis:
    A new methodology for prenylation of thiol compounds has been developed. The approach is based on the use of prenyl sulfates as new reagents for S-prenylation of benzenethiol and cysteamine in aqueous systems. The C10-prenols geraniol and nerol that differ in the configuration (E or Z, correspondingly) of the α-isoprene unit were efficiently O-sulfated in the presence of a pyridine-SO3' complex. The obtained geranyl and neryl sulfates were tested as alkylating agents. These compounds were chosen to reveal the influence of the α-isoprene unit configuration on their alkylation (prenylation) ability. S-Geranyl cysteine was prepared to demonstrate the applicability of this method for prenylation of peptides containing mercapto amino acids.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 807-813
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Non-racemic mixture model: a computational approach
    Autorzy:
    Polanco, Carlos
    Buhse, Thomas
    Powiązania:
    https://bibliotekanauki.pl/articles/1038677.pdf
    Data publikacji:
    2017
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    origin of homochirality
    prebiotic peptide formation
    chiral asymmetry
    amino acids
    Opis:
    The behavior of a slight chiral bias in favor of l-amino acids over d-amino acids was studied in an evolutionary mathematical model generating mixed chiral peptide hexamers. The simulations aimed to reproduce a very generalized prebiotic scenario involving a specified couple of amino acid enantiomers and a possible asymmetric amplification through autocatalytic peptide self-replication while forming small multimers of a defined length. Our simplified model allowed the observation of a small ascending but not conclusive tendency in the l-amino acid over the d-amino acid profile for the resulting mixed chiral hexamers in computer simulations of 100 peptide generations. This simulation was carried out by changing the chiral bias from 1% to 3%, in three stages of 15, 50 and 100 generations to observe any alteration that could mean a drastic change in behavior. So far, our simulations lead to the assumption that under the exposure of very slight non-racemic conditions, a significant bias between l- and d-amino acids, as present in our biosphere, was unlikely generated under prebiotic conditions if autocatalytic peptide self-replication was the main or the only driving force of chiral auto-amplification.
    Źródło:
    Acta Biochimica Polonica; 2017, 64, 1; 17-19
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Phosphorylation of basic amino acid residues in proteins: important but easily missed
    Autorzy:
    Cieśla, Joanna
    Frączyk, Tomasz
    Rode, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1039902.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    basic amino acids
    posttranslational modification
    phosphorylation
    acid-labile
    base-stable
    phosphoramidate
    Opis:
    Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine, arginine and lysine residues also may undergo phosphorylation to yield acid-labile phosphoramidates, most often remaining undetected in conventional studies of protein phosphorylation. It has become increasingly evident that acid-labile protein phosphorylations play important roles in signal transduction and other regulatory processes. Beside acting as high-energy intermediates in the transfer of the phosphoryl group from donor to acceptor molecules, phosphohistidines have been found so far in histone H4, heterotrimeric G proteins, ion channel KCa3.1, annexin 1, P-selectin and myelin basic protein, as well as in recombinant thymidylate synthase expressed in bacterial cells. Phosphoarginines occur in histone H3, myelin basic protein and capsidic protein VP12 of granulosis virus, whereas phospholysine in histone H1. This overview of the current knowledge on phosphorylation of protein basic amino-acid residues takes into consideration its proved or possible roles in cell functioning. Specific requirements of studies on acid-labile protein phosphorylation are also indicated.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 2; 137-148
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    DALDA analogues containing α-hydroxymethylamino acids.
    Autorzy:
    Olma, Aleksandra
    Chung, Nga
    Schiller, Peter
    Zabrocki, Janusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1044058.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    amphiphilic amino acids
    α-hydroxymethylamino acids
    DALDA analogues
    opioid activity in vitro
    opioid peptides
    Opis:
    To evaluate the role of aromatic amino-acids residues, four analogues of the μ-selec-tive opioid peptide agonist DALDA (H-Tyr-D-Arg-Phe-Lys-NH2) containing the amphiphilic, α,α-disubstituted amino acid (R)- or (S)-α-hydroxymethyltyrosine (HmTyr) in position 1 and (R)- or (S)-α-hydroxymethylphenylalanine (HmPhe) in position 3 of the peptide sequence were synthesized. Only the [(R)-HmPhe3)]DALDA analogue displayed full agonistic activity in both the guinea pig ileum and the mouse vas deferens assays and turned out to be a δ receptor-selective opioid agonist.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 1121-1124
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    A toy model of prebiotic peptide evolution: the possible role of relative amino acid abundances
    Autorzy:
    Polanco, Carlos
    Buhse, Thomas
    Samaniego, José
    Castañón González, Jorge
    Powiązania:
    https://bibliotekanauki.pl/articles/1039570.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    polarity index method.
    computer simulation
    prebiotic polymerization
    toy model
    peptides
    amino acids
    Opis:
    This paper presents a mathematical-computational toy model based on the assumed dynamic principles of prebiotic peptide evolution. Starting from a pool of amino acid monomers, the model describes in a generalized manner the generation of peptides and their sequential information. The model integrates the intrinsic and dynamic key elements of the initiation of biopolymerization, such as the relative amino acid abundances and polarities, as well as the oligomer reversibility, i.e. fragmentation and recombination, and peptide self-replication. Our modeling results suggest that the relative amino acid abundances, as indicated by Miller-Urey type electric discharge experiments, played a principal role in the early sequential information of peptide profiles. Moreover, the computed profiles display an astonishing similarity to peptide profiles observed in so-called biological common ancestors found in the following three microorganisms; E. coli, M. jannaschii, and S. cereviasiae. The prebiotic peptide fingerprint was obtained by the so-called polarity index method that was earlier reported as a tool for the identification of cationic amphipathic antibacterial short peptides.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 2; 175-182
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structure and function relationships of proteins based on polar profile: a review
    Autorzy:
    Polanco, Carlos
    Buhse, Thomas
    Uversky, Vladimir
    Powiązania:
    https://bibliotekanauki.pl/articles/1038800.pdf
    Data publikacji:
    2016
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    amino acids
    polarity profile
    pattern recognition
    dynamical systems theory
    atherosclerosis
    selective antibacterial peptides
    intrinsically disordered proteins
    Opis:
    Proteins in the post-genome era impose diverse research challenges, the main are the understanding of their structure-function mechanism, and the growing need for new pharmaceutical drugs, particularly antibiotics that help clinicians treat the ever- increasing number of Multidrug-Resistant Organisms (MDROs). Although, there is a wide range of mathematical-computational algorithms to satisfy the demand, among them the Quantitative Structure-Activity Relationship algorithms that have shown better performance using a characteristic training data of the property searched; their performance has stagnated regardless of the number of metrics they evaluate and their complexity. This article reviews the characteristics of these metrics, and the need to reconsider the mathematical structure that expresses them, directing their design to a more comprehensive algebraic structure. It also shows how the main function of a protein can be determined by measuring the polarity of its linear sequence, with a high level of accuracy, and how such exhaustive metric stands as a "fingerprint" that can be applied to scan the protein regions to obtain new pharmaceutical drugs, and thus to establish how the singularities led to the specialization of the protein groups known today.
    Źródło:
    Acta Biochimica Polonica; 2016, 63, 2; 229-233
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-9 z 9

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