83 resultados para Single Amino-acid


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P>The non-classical major histocompatibility complex (MHC) class I molecule CD1d presents lipid antigens to invariant natural killer T (iNKT) cells, which are an important part of the innate immune system. CD1d/iNKT systems are highly conserved in evoluti

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We reported here four structures of lanthanide-amino acid complexes obtained under near physiological pH conditions and their individual formula can be described as [Tb-2(DL-Cys)(4)(H2O)(8)]Cl-2 (1), [Eu-4(mu(3)-OH)(4)(L-Asp)(2)(L-HAsp)(3)(H2O)(7)] Cl center dot 11.5H(2)O (2), [Eu-8-(L-HVal) (16)(H2O)(32)]Cl-24 center dot 12.5H(2)O (3), and [Tb-2(DL-HVal)(4)(H2O)(8)]Cl-6 center dot 2H(2)O (4). These complexes showed diverse structures and have shown potential application in DNA detection. We studied the interactions of the complexes with five single-stranded DNA and found different fluorescence enhancement, binding affinity and binding stoichiometry when the complexes are bound to DNA.

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Different DNA selectivity was found for the newly synthesized europium-L-valine complex. Unexpected DNA and RNA selection results showed that europium-L-valine complex can cause single-stranded polydA and polyrA to self-structure. The sigmoidal melting curve profiles indicate the transition is cooperative, similar to the cooperative melting of a duplex DNA. This is different from another europium amino acid complex, europium-L-aspartic acid complex which can induce B-Z transition under the low salt condition. To our knowledge, there is no report to show that a metal-amino acid complex can cause the self-structuring of single-stranded DNA and RNA.

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A novel compound was synthesized and characterized by means of elemental analysis, IR and UV spectra, TG, CV and single crystal X-ray diffraction. The compound crystallized in an orthorhombic space group C222 with a=1. 622 4(3) nm, b=3. 498 4(7) nm, c=1. 301 5(3) nm, V=7. 387 (3) nm(3), Z=6, R-1= 0. 037 3, wR(2)=0. 114 0. The Ala (Ala = alanine) molecules were protonated at the amino nitrogen N (1) and the C (2) of Ala group with the terminal oxygen atom O(15), O(14), O(26) and O(27) of the polyoxometalates participating in the hydrogen bond network. The anti-tumor activity of the title compound was estimated against Hela and Pc-3m cancer cells.

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The novel amino-acid-containing polyoxometalate Ka(6) [Cu(Ala)(2) (H2O)(2)](2) [Cu-4 (H2O)(2) . (AsW9O34)(2)] . 16H(2)O was synthesized from the reaction of K-10[Cu-4(H2O)(2)(AsW9O34)(2)] . 20H(2)O with beta -alanine, Its structure has been determined by single crystal X-ray diffraction. It crystallizes in the triclinic space group P (1) over bar, with a=1. 196 3(2) nm, b=1. 536 5(3) nm, c=1. 591 4(3) nm, alpha =93. 97(3)degrees, beta= 110. 88(3)degrees, gamma =101. 07(3)degrees, V=2. 651 8(9) nm(3) and Z=1. Least-squares refinement of the structure leads to R and R-w factors of 0. 067 3 and 0. 162 8, respectively. An unusual structural feature of the compound is that the polyanion [Cu-4(H2O)(2) (AsW9O34)](10-) is linked with the amino-acid complex of Cu2+ by a mu -oxygen atom.

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Amino acid substitution matrices play an essential role in protein sequence alignment, a fundamental task in bioinformatics. Most widely used matrices, such as PAM matrices derived from homologous sequences and BLOSUM matrices derived from aligned segments of PROSITE, did not integrate conformation information in their construction. There are a few structure-based matrices, which are derived from limited data of structure alignment. Using databases PDB_SELECT and DSSP, we create a database of sequence-conformation blocks which explicitly represent sequence-structure relationship. Members in a block are identical in conformation and are highly similar in sequence. From this block database, we derive a conformation-specific amino acid substitution matrix CBSM60. The matrix shows an improved performance in conformational segment search and homolog detection.

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Receptor/ligand interactions are basic issues to cell adhesion, which are important to many physiological and pathological processes such as lymphocyte-mediated cytotoxicity, tumor metastasis and inflammatory reactionl. Selectin/carbohydrate ligand bindings have been found to mediate the fast rolling of leukocytes on activated endothelial monolayer. Kinetic rate and binding affinity constants are essential determinants of cell adhesion...

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A novel L-amino acid oxidase, named TSV-LAO, has been purified and cloned from the snake Trimeresurus stejnegeri. Fifty percentage cytotoxic concentrations (CC50) of TSV-LAO on C8166 cells were 24 and 390 nM in the absence or presence of catalase (400nM), respectively. However, at concentrations that showed little effect on cell viability, TSV-LAO displayed dose dependent inhibition on HIV-1 infection and replication. The antiviral selectivity indexes (CC50/EC50) were 16 and 6, respectively, corresponding to the measurements of syncytium formation and HIV-1 p24 antigen expression. Interestingly, the presence of catalase resulted in an increase of its antiviral selectivity to 52 and 38. Under the same conditions, no anti-HIV-1 activity was observed by exogenous addition of H2O2. The complete amino acid sequence of TSV-LAO, as deduced from its cDNA, exhibits a high degree of sequence identity with other snake venom LAOs. (C) 2003 Elsevier Inc. All rights reserved.

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An L-amino acid oxidase from Ophiophagus hannah snake venom (Oh-LAAO) was purified by successive gel filtration, ion-exchange and heparin chromatography. Oh-LAAO did not induce platelet aggregation; however, it had potent inhibitory activity on platelet a

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An L-amino acid oxidase (LAAO), NA-LAAO, was purified from the venom of Naja atra. Its N-terminal sequence shows great similarity with LAAOs from other snake venoms. NA-LAAO dose-dependently induced aggregation of washed human platelets. However, it had n

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A new L-amino acid oxidase (designated as DRS-LAAO) was purified from Daboia russellii siamensis venom by ion-exchange, gel filtration and affinity chromatographies. DRS-LAAO is a homodimeric enzyme with a molecular weight of 120.0 kDa as measured by size

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An L-amino acid oxidase (TM-LAO) from the venom of Hunan Trimeresurus mucrosquamatus was purified to homogenicity by three steps including DEAE Sephadex A-50 ion-exchange chromatography, Sephadex G-75 gel filtration and Resourse Q ion-exchange chromatography. TM-LAO is composed of two identical subunits with a molecular weight of 55 kD by SDS-polyacrylamide gel electrophoresis. The molecular weight was different with that of LAO purified from the same species distributed in Taiwan that was 70 kD. The 24 N-terminal ammo acid sequence of TM-LAO is ADNKNPLEECFRETNYEEFLEIAR, which shares high similarity with other Viperid snake venom LAOs and has moderate similarity with Elapid snake venom LAOs. Further studies found that TM-LAO inhibited the growth of E. colt, S. aurues and B. dysenteriae. TM-LAO also showed cytotoxicity and platelet aggregation activity. All the biological activities were eliminated by catalase, a H2O2 scavenger. It shows that these biological effects are possibly due to the formation of H2O2 produced by TM-LAO.