Biospectroscopy最新文献

{"title":"Special issue on “hot topics” from the ECSBM'97 conference","authors":"Pedro Carmona,&nbsp;Ronald E. Hester","doi":"10.1002/(SICI)1520-6343(1998)4:5+<S1::AID-BSPY1>3.0.CO;2-W","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5+<S1::AID-BSPY1>3.0.CO;2-W","url":null,"abstract":"","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 S5","pages":"S1"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5+<S1::AID-BSPY1>3.0.CO;2-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"110257088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In vitro and in vivo Raman spectroscopy of human skin","authors":"P. J. Caspers,&nbsp;G. W. Lucassen,&nbsp;R. Wolthuis,&nbsp;H. A. Bruining,&nbsp;G. J. Puppels","doi":"10.1002/(SICI)1520-6343(1998)4:5+<S31::AID-BSPY4>3.0.CO;2-M","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5+<S31::AID-BSPY4>3.0.CO;2-M","url":null,"abstract":"<p>Noninvasive techniques that provide detailed information about molecular composition, structure, and interactions are crucial to further our understanding of the relation between skin disease and biochemical changes in the skin, as well as for the development of penetration enhancers for transdermal drug administration. In this study we present <i>in vitro</i> and <i>in vivo</i> Raman spectra of human skin. Using a Raman microspectrometer, <i>in vitro</i> spectra were obtained of thin cross sections of human skin. They provided insight into the molecular composition of different skin layers. Evidence was found for the existence of a large variation in lipid content of the stratum corneum. A simple experimental setup for <i>in vivo</i> confocal Raman microspectroscopy of the skin was developed. <i>In vivo</i> Raman spectra of the stratum corneum were obtained at different positions of the arm and hand of three volunteers. They provided evidence for differences in the concentration of natural moisturizing factor at these positions. © 1998 John Wiley &amp; Sons, Inc. Biospectroscopy 4: S31–S39, 1998</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 S5","pages":"S31-S39"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5+<S31::AID-BSPY4>3.0.CO;2-M","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701169","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fluorescent properties of amino acids labeled with ortho-aminobenzoic acid","authors":"Amando S. Ito,&nbsp;Rozane De F. Turchiello,&nbsp;Isaura Y. Hirata,&nbsp;Maria Helena S. Cezari,&nbsp;Morten Meldal,&nbsp;Luiz Juliano","doi":"10.1002/(SICI)1520-6343(1998)4:6<395::AID-BSPY4>3.0.CO;2-Y","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:6<395::AID-BSPY4>3.0.CO;2-Y","url":null,"abstract":"<p><i>ortho</i>-Aminobenzoic acid (Abz) has been used as a convenient fluorescent donor group in internally quenched fluorescent peptides, which are employed as substrates for several proteolytic enzymes. As Abz is usually bound to the N-amino terminal of these peptides, it is of interest to investigate the Abz group fluorescent properties bound to different amino acids. We report in this article the optical absorption and fluorescent properties, in aqueous media, of Abz bound to the α-amino group of Ala, Gly, Leu, Ile, Val, Pro, Phe, Arg, Glu, Met, Asn, Tyr, and Trp, with monomethyl-amidated α-carboxyl group. In order to explore the origin of the drastic reduction of Abz attached to N^α amino group of prolyl-peptides, we also examined the fluorescence properties of Abz-NHCH₃, Abz-N(CH₃)₂, and Abz-pyrrolidine. Molecular dynamics simulation and NMR data indicated a lack of periplanarity of the Abz-dimethylamide, which could be the origin of low fluorescence quantum yield of Abz-prolyl-peptides. © 1998 John Wiley &amp; Sons, Inc. Biospectroscopy 4: 395–402, 1998</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 6","pages":"395-402"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:6<395::AID-BSPY4>3.0.CO;2-Y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78660333","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Surface-enhanced Raman scattering and fluorescence spectroscopy reveal molecular interactions of all-trans retinoic acid and RARγ ligand-binding domain","authors":"H. Morjani,&nbsp;A. Beljebbar,&nbsp;G. D. Sockalingum,&nbsp;T. A. Mattioli,&nbsp;D. Bonnier,&nbsp;H. Gronemeyer,&nbsp;M. Manfait","doi":"10.1002/(SICI)1520-6343(1998)4:5<297::AID-BSPY1>3.0.CO;2-6","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5<297::AID-BSPY1>3.0.CO;2-6","url":null,"abstract":"<p>Surface-enhanced Raman scattering and fluorescence were used to investigate the interactions of all-<i>trans</i> retinoic acid with the gamma-type retinoic acid receptor. Raman data revealed a significant attenuation in intensity of the bands originating from the retinoic acid polyenic chain upon receptor binding, with the spectrum being dominantly that of the β-ionone ring. Fluorescence measurements supported the hydrophobic character of the ligand binding. These novel spectroscopic results are fully consistent with the published X-ray crystallographic data and suggest that these techniques may be valuable additional tools to characterize the interactions of agonists and antagonists with residues in the ligand-binding pockets of retinoid receptor homo- and heterodimers. © 1998 John Wiley &amp; Sons, Inc. Biospectroscopy 4: 297–302, 1998</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 5","pages":"297-302"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5<297::AID-BSPY1>3.0.CO;2-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73236991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of soybean seed coat peroxidase: Resonance Raman evidence for a structure-based classification of plant peroxidases","authors":"Mikkel Nissum,&nbsp;Alessandro Feis,&nbsp;Giulietta Smulevich","doi":"10.1002/(SICI)1520-6343(1998)4:6<355::AID-BSPY1>3.0.CO;2-I","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:6<355::AID-BSPY1>3.0.CO;2-I","url":null,"abstract":"<p>Electronic absorption and resonance Raman spectra of ferric and ferrous forms of a peroxidase from soybean seed coat (SBP) at neutral and alkaline pH values together with the spectra of the ferric-fluoride complex are reported. At neutral pH a quantum mechanically mixed spin state, resulting from the admixture of intermediate spin, <i>S</i> = 3/2, and high spin, <i>S</i> = 5/2, configurations, has been identified which coexists with five- and six-coordinate high-spin hemes. A complete conversion to a fluoride-ligated six-coordinate high-spin and a hydroxy-ligated six-coordinate low-spin heme are observed at acid pH in the presence of fluoride and at alkaline pH, respectively. The spectral features suggest that both the fluoride and hydroxo ligands are stabilized by hydrogen-bond interactions with the distal Arg residue and through a water molecule with the distal His residue. The ferrous form shows a single ν(Fe—Im) at 246 cm⁻¹ at neutral pH. The data indicate that SBP shares many characteristics with peroxidases belonging to class III of the “plant peroxidase” superfamily. © 1998 John Wiley &amp; Sons, Inc. Biospectroscopy 4: 355–364, 1998</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 6","pages":"355-364"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:6<355::AID-BSPY1>3.0.CO;2-I","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20760938","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"On the use of ultraviolet resonance Raman intensities to elaborate molecular force fields: Application to nucleic acid bases and aromatic amino acid residues models","authors":"P. Lagant,&nbsp;G. Vergoten,&nbsp;W. L. Peticolas","doi":"10.1002/(SICI)1520-6343(1998)4:6<379::AID-BSPY3>3.0.CO;2-2","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:6<379::AID-BSPY3>3.0.CO;2-2","url":null,"abstract":"<p>Normal modes analyses for different molecules with biological interest have been performed and checked via the calculation of resonance Raman intensities. For this purpose, molecular orbital calculations were used to determine bond order changes in the lowest-lying electronic transitions. These bond order changes were used to calculate resonance Raman intensities in order to obtain correct vibrational assignments and reliable force fields. © 1998 John Wiley &amp; Sons, Inc. Biospectroscopy 4: 379–393, 1998</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 6","pages":"379-393"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:6<379::AID-BSPY3>3.0.CO;2-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20760940","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure/activity studies of the anti-MUC1 monoclonal antibody C595 and synthetic MUC1 mucin-core-related peptides and glycopeptides.","authors":"D I Spencer,&nbsp;S Missailidis,&nbsp;G Denton,&nbsp;A Murray,&nbsp;K Brady,&nbsp;C I Matteis,&nbsp;M S Searle,&nbsp;S J Tendler,&nbsp;M R Price","doi":"10.1002/(SICI)1520-6343(1999)5:2<79::AID-BSPY2>3.0.CO;2-#","DOIUrl":"https://doi.org/10.1002/(SICI)1520-6343(1999)5:2<79::AID-BSPY2>3.0.CO;2-#","url":null,"abstract":"<p><p>MUC1 mucin is a large complex glycoprotein expressed on normal epithelial cells in humans and overexpressed and under or aberrantly glycosylated on many malignant cancer cells which consequently allows recognition of the protein core by antibodies. In order to understand how glycosylation may modulate or regulate antibody binding of mucin protein core epitopes, we have analyzed the antibody C595 (epitope RPAP) for its structure, stability, and its binding to a series of synthetic peptides and glycopeptides by a number of spectroscopic methods. Thermal and pH denaturation studies followed by changes in the CD spectrum of the antibody indicate critical involvement of specific residues to the stability of the antibody. Fluorescence binding studies indicate that alpha-N-acetylgalactosamine (GalNAc) glycosylation of a MUC1 mucin synthetic peptide TAPPAHGVT9SAPDTRPAPGS20T21APPA at threonine residues 9 and 21 and serine residue 20 enhanced the binding of antibody. The structural effects of GalNAc glycosylation on the conformation of the MUC1 peptide were studied. CD of the peptides and glycopeptides in a cryogenic mixture cooled to approximately -97 degrees C revealed that a left-handed polyproline II helix (PPII) is adopted by the peptides in solution, which appears to be further stabilized by addition of the GalNAc residues. Consistent with the PPII helical structure, which has no intra-amide hydrogen bonds, high-field NMR spectroscopy of the glycopeptide revealed no sequential dNN, medium-range, or long-range nuclear Overhauser effect (NOE) connectivities. These studies indicate that stabilization of the PPII helix by GalNAc glycosylation present the epitope of C595 antibody with a favorable conformation for binding. Furthermore, they illustrate that glycosylation of the MUC1 tumor marker protein with a simple O-linked saccharide expressed in many cancers, can enhance the binding of the clinically relevant C595 antibody.</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 2","pages":"79-91"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:2<79::AID-BSPY2>3.0.CO;2-#","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21087778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biological effects of rare earth protein complexes: influence of lanthanide ions Eu3+, Tb3+ on secondary structure of calmodulins.","authors":"Y Y Song,&nbsp;Y Z Xu,&nbsp;S F Weng,&nbsp;L B Wang,&nbsp;X F Li,&nbsp;T F Zhang,&nbsp;J G Wu","doi":"10.1002/(SICI)1520-6343(1999)5:6<371::AID-BSPY6>3.0.CO;2-#","DOIUrl":"https://doi.org/10.1002/(SICI)1520-6343(1999)5:6<371::AID-BSPY6>3.0.CO;2-#","url":null,"abstract":"<p><p>The secondary structure of four kinds of calmodulins (CaMs; i.e., Brassica campestris pollen CaM, bovine brain CaM, earthworm calcium binding protein, and earthworm new calcium binding protein) in thin films are determined by the FTIR resolution enhanced technique and curve fitting. The variation in the secondary structure of CaM upon its binding with Ca2+, Eu3+, and Tb3+, the assay of phosphodiesterase enzyme, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis are also investigated. The effect of lanthanide ions on the conformation of CaM are described.</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"371-7"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<371::AID-BSPY6>3.0.CO;2-#","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21463168","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biodeterioration of granite monuments by Ochrolechia parella (L.) mass: an FT Raman spectroscopic study.","authors":"B Prieto,&nbsp;M R Seaward,&nbsp;H G Edwards,&nbsp;T Rivas,&nbsp;B Silva","doi":"10.1002/(SICI)1520-6343(1999)5:1<53::AID-BSPY7>3.0.CO;2-#","DOIUrl":"https://doi.org/10.1002/(SICI)1520-6343(1999)5:1<53::AID-BSPY7>3.0.CO;2-#","url":null,"abstract":"<p><p>Ochrolechia parella is one of the most abundant lichens colonizing granite monuments in the region of Galicia (N.W. Spain). Its interaction with granite used in the construction of four ancient monuments was studied using FT Raman spectroscopy to evaluate the production of calcium oxalate by this lichen and the relationship of this production with different environmental conditions, particularly humidity. The results obtained showed that Ochrolechia parella is an aggressive colonizer, causing chemical disturbances to the granite through the formation of both calcium oxalate monohydrate and dihydrate. Apothecial development appears to be related to the production of calcium oxalate, and humidity determines the state of hydration of the calcium oxalate in the thallus.</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 1","pages":"53-9"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:1<53::AID-BSPY7>3.0.CO;2-#","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21090722","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Separable contributions of ordered and disordered lipid fatty acyl chain segments to nuCH2 bands in model and biological membranes: a Fourier transform infrared spectroscopic study.","authors":"Z Kóta,&nbsp;M Debreczeny,&nbsp;B Szalontai","doi":"10.1002/(SICI)1520-6343(1999)5:3<169::AID-BSPY6>3.0.CO;2-#","DOIUrl":"https://doi.org/10.1002/(SICI)1520-6343(1999)5:3<169::AID-BSPY6>3.0.CO;2-#","url":null,"abstract":"<p><p>In this article, the assignment of the nu(C-H) stretching region of lipid molecules is revisited. This region is extensively used to follow lipid phase transitions, and especially the frequency shifts and bandwidth alterations in the nu(sym)CH2 band have been utilized in this respect. Here, we propose and prove that behind these phenomena there are pairs of component bands in the cases of both the nu(sym)CH2 and the nu(as)CH2 bands. The lower-frequency components of the pairs are assigned to the vibrations of CH2 groups on trans segments of the fatty acyl chains, while the higher-frequency components of the pairs are assigned to CH2 groups on gauche segments. To prove these assignments, we have shown that the nuCH2 frequencies are characteristic of the conformation of the lipid fatty acyl chain itself, and not the state of the whole lipid matrix. Curve fitting in fact revealed the conformer-specific components. With the use of singular value decomposition analysis we have demonstrated that the relative intensity changes in the components, and not the shifts in the whole bands, cause the observed shifts in the nuCH2 bands upon lipid phase transition. The results of this approach are presented for deuterium-saturated dioleoyl-phosphatidylcholine mixtures, for the gel --> liquid-crystalline phase transition of dipalmitoyl-phosphatidylcholine multilayers, and for a biological membrane, barley thylakoid. This refined assignment offers physically plausible reasoning for the observed phenomena and is able to explain frequency shifts and bandwidth changes observed previously upon lipid phase transitions, including their nonconcerted temperature dependences. In biological membranes, this interpretation allows the separation of protein- and membrane-dynamics-induced lipid conformational changes.</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 3","pages":"169-78"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:3<169::AID-BSPY6>3.0.CO;2-#","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21248170","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}