Biomedical Spectroscopy and Imaging最新文献

{"title":"Cholesterol: Revisiting its fluorescent journey on 200th anniversary of Chevruel’s “cholesterine”","authors":"Arunima Chaudhuri, Deepak Anand","doi":"10.3233/BSI-170166","DOIUrl":"https://doi.org/10.3233/BSI-170166","url":null,"abstract":"The legacy of Micheal Chevruel’s discovery of “cholesterine” as a non-saponifiable lipid from gall stones has ignited the imagination and research of countless minds for over two centuries now. In this review, we have provided a brief chronicle of the early history of cholesterol research which paved the way to present day understanding of membrane biology. We have discussed the properties and functionality of various fluorescent analogs of cholesterol in view of the ultra-high sensitivity, rapid response and spatial resolution obtained using fluorescence spectroscopic, microscopic and flow cytometric techniques. The repertoire of fluorescent analogs discussed for cholesterol research include the naturally occurring analogs (dehydroergosterol and cholestatrienol); polarity sensitive probes (NBDand dansyl-cholesterol); bright and photostable probe (BODIPY-cholesterol); clickable alkyne cholesterol and cholesterol binding macromolecules (fluorescently labeled non-toxic subunits of perfringolysin O and filipin) in monitoring cholesterol content in live and fixed cells. We have elaborated on the applications of the fluorescent analogs of cholesterol in clinical research, taking atherosclerosis, Niemann–Pick C and Alzheimer’s disease as representative examples. The applicability of fluorescent probes of cholesterol has become more relevant with the advent of various super-resolution microscopic techniques today and holds the promise of shedding light into the molecular orchestra of lipid-protein interaction with nanometer-scale resolution.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-170166","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69857105","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":"Infrared spectroscopy as a new tool for studying single living cells: Is there a niche?","authors":"S. Sabbatini, C. Conti, G. Orilisi, E. Giorgini","doi":"10.3233/BSI-170171","DOIUrl":"https://doi.org/10.3233/BSI-170171","url":null,"abstract":"FTIR spectroscopy is an analytical technique widely applied for studying the vibrational fingerprint of organic compounds. In recent years, it has been applied to many biomedical fields because of its potential to detect the composition and molecular structure of various biological materials without the need of probe molecules. The coupling of IR spectrometers with visible microscopes has led to perform the imaging analysis of non-homogeneous samples, such as tissues and cells, in which the biochemical and spatial information are close related. In this review, we report the most significant applications of FTIR to the study of cells in different conditions (fixed, dried and living) with the aim to monitor their biochemical modifications, either induced or naturally occurring.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-170171","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69857196","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":"The correlation of plasma proteins binding capacity and flavopiridol cellular and clinical trial studies","authors":"Daniel P Myatt","doi":"10.3233/BSI-170165","DOIUrl":"https://doi.org/10.3233/BSI-170165","url":null,"abstract":"Previous clinical research has suggested high-affinity binding of flavopiridol (FLAP) to human blood serum proteins, specifically either human serum albumin (HSA) or human alpha-1-acid glycoprotein (hAGP), when compared to fetal bovine serum albumin (BSA) or bovine alpha-1-acid glycoprotein (bAGP) used in pre-clinical assays. This high-affinity binding was suggested as the reason for its poor human clinical trial performance as a treatment for chronic lymphocytic leukaemia (CLL). Using three biophysical techniques, specifically circular dichroism (CD), isothermal calorimetry (ITC) and fluorescence spectroscopy, I show that FLAP does not have an overly high-affinity for either fetal BSA, HSA, bAGP or hAGP. I therefore suggest an alternate hypothesis that models the albumin and alpha-1-acid glycoprotein (AGP) binding sites at the different protein concentrations used in the fetal bovine pre-clinical assay and human physiological conditions. I use analytical ultracentrifugation (AUC) experiments to determine the validity of the theoretical models. The models can also be altered to account for the elevated AGP levels and reduced albumin levels seen in human cancer patients. Major differences in the concentrations of free available FLAP are observed between the fetal bovine pre-clinical model and human physiological conditions. A number of recommendations can therefore be made on how future pre-clinical assay studies should be conducted.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-170165","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856990","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":"Cholesterol: A chemical of life and death.","authors":"P. Haris","doi":"10.3233/BSI-160161","DOIUrl":"https://doi.org/10.3233/BSI-160161","url":null,"abstract":"A Google search for “cholesterol” (December 2016) returned 73,300,000 hits. This is much higher compared to 9,680,000 and 14,500,000 hits for “haemoglobin” (UK spelling) and “hemoglobin” (USA spelling), respectively. There is little doubt that cholesterol is one of the most well known biochemical substances in the world. Unfortunately, to the vast majority of the people, it is associated with death due to its connection with cardiovascular disease (CVD) which is the number one cause for death globally [2]. A Google search (December 2016) for “death” and “cholesterol” returned 32,700,000 hits in contrast to 37,400,000 hits when “life” and “cholesterol” was combined. The huge number of hits linked to death is surprising, although it is understandable considering the association of cholesterol with CVD. The Google results should be treated with caution but there is no doubt that cholesterol has a negative image and it is seen by many as a molecule of disease and death, and everything possible should be done to reduce its intake through the diet. Unfortunately, this link to disease and death leads people to overlook the fact cholesterol is also essential for human life. It plays a pivotal role in the structural organisation of biological membranes, tissue repair and as a precursor to a range of hormones and synthesis of vitamin D. Cholesterol was first identified in gallstones in about 1758 by the French scientist François Poulletier de la Salle. However, it was another French scientist, Michel-Eugène Chevreul (see Fig. 1), who first named this compound as “cholesterine” at a meeting of the French Academy of Sciences on August 26, 1816 [5]. Subsequently, it was identified to be an alcohol and was called cholesterol. Chevreul was born in Angers, France in 1786 and died in Paris in 1889. He is credited with being the founding father of research on fats and oils. This year (2016) marks the 200th anniversary of the naming of this compound and to celebrate this notable occasion, I chose to produce a special issue of Biomedical Spectroscopy and Imaging devoted to cholesterol research. The issue is dedicated to the memory of my former PhD supervisor, the late Professor Dennis Chapman FRS, who was one of the first to demonstrate the role of cholesterol in modulating membrane fluidity [4,7]. It contains a number of articles from researchers who are applying diverse techniques, including spectroscopic and imaging methods, to explore the structure and function of cholesterol. Ever since it was named in 1816, numerous scientists have engaged in research to understand the structure and function of this small hydrophobic molecule. It is worthy of being described as the “the most highly decorated small molecule in biology” [3]. The scientific community have certainly appreciated the value of this molecule and 13 Nobel Prizes have been awarded to scientists who have worked on cholesterol [3]. The first of these prizes was awarded in 1928 to Windaus and Wieland who d","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-12-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160161","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69857294","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":"Kenneth J. Rothschild - A pioneer of infrared difference spectroscopy of membrane proteins","authors":"P. Haris","doi":"10.3233/BSI-160150","DOIUrl":"https://doi.org/10.3233/BSI-160150","url":null,"abstract":"Kenneth J. Rothschild’s (see Fig. 1) interest in science and specifically spectroscopy began at an early age. In my personal communication with Ken, he told me that as a high school student (1961– 1965), at Raritan High School (Hazlet, NJ, USA), he built a spectroscopic device for identifying different compounds. Between 1965–1969, Ken was an undergraduate student at Rensselaer Polytechnic Institute (RPI) where he majored in Physics. During this period he had some notable achievements. This included","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160150","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856555","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":"Thirty years of European Conference on Spectroscopy of Biological Molecules celebrated in Ruhr University Bochum","authors":"P. Haris, K. Gerwert","doi":"10.3233/BSI-160142","DOIUrl":"https://doi.org/10.3233/BSI-160142","url":null,"abstract":"The 16th European Conference on Spectroscopy of Biological Molecules (ECSBM) was held at Ruhr University Bochum in Germany (6–10 September, 2015). The conference was chaired by Klaus Gerwert (see Fig. 1) and it coincided with the 30th year of this conference series. The conference is held in alternate years in different countries within Europe. The first ECSBM was held at the University of Reims in September 1985. It was organised by Lucien Bernard (Rector Reims University) and his colleagues Alain Alix and Michel Manfait. In total three out of the 16th ECSBM conferences has been held in Germany and this reflects the large number of German scientists and institutions that focus on application of spectroscopy in biological research. The second ECSBM meeting was held in Freiburg, Germany, in September 1987 and after 18 years, in 2005, the conference returned back to Germany once more. The meeting was held than in Aschaffenburg. It is noteworthy that the 16th ECSBM conference in Bochum was a form of reunion for key scientists who were responsible for starting this conference series including Prof. Werner Mäntele (see Fig. 1). Werner, who is currently based at the Johann Wolfgang Goethe University Frankfurt am Main, was awarded the Life Time Achievement Award at the Bochum meeting for his outstanding contributions in the field of biological vibrational spectroscopy. The conference in Bochum now (see Fig. 1) had a total of 222 participants from 26 different countries covering the continents of Europe, Asia and America. There were 69 lectures (15 invited lectures, 18 contributed talks and 36 selected talks from submitted abstracts). This special issue of Biomedical Spectroscopy and Imaging presents a selection of work presented at the conference. It provides excellent examples of application of spectroscopic and imaging techniques for the study of diverse biological systems. The conference in Bochum was dominated by impressive presentations which show how vibrational spectroscopy is used at different scales to solve biological questions. The talks demonstrated in a convincing manner how the use of time-resolved FTIR difference spectroscopy is able to determine molecular reaction mechanisms of proteins and protein interactions at the atomic level. For example the molecular reaction mechanisms of retinal-proteins like bacteriorhodopsin and channelrhodopsins and","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160142","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856545","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":"Raman spectroscopic characterisation of photo-active keratin doped with Methylene Blue for wound dressings and tissue engineering","authors":"A. Aluigi, G. Sotgiu, A. Torreggiani, R. Zamboni, A. Guerrini, G. Varchi, V. Orlandi","doi":"10.3233/BSI-160143","DOIUrl":"https://doi.org/10.3233/BSI-160143","url":null,"abstract":"BACKGROUND: The design of wound dressings with extraordinary functionalities that fully address the problem of wound healing is an ambitious challenge in biomedical field. Keratin is a protein most abundant in nature, being the major component of wool, feather, hair, etc., with promising applications in biomedical and regenerative medicine fields. A high level of antibacterial functionality is another desirable property for applications in biomedical field in response to the increasing resistance of bacteria to antibiotics. One of the emerging methods of disinfection and sterilization is the antimicrobial photodynamic therapy (APDT), which uses light combined to a photosensitizer and oxygen to produce phototoxic species. OBJECTIVE: Biomatrices (photo-active keratin) made of wool keratin functionalized with methylene blue, a powerful photosensitizer, have been developed and tested as systems that combine the bioactive properties with the antimicrobial photodynamic functionality. METHODS: The biomatrix resistance to photo-degradation and the formation of reactive oxygen species were evaluated by spectroscopic methods, whereas the antibacterial properties were tested towards gram-positive bacteria. RESULTS: The Raman analysis revealed that specific damages occur at sensitive amino acid sites, selectively, rather than indiscriminately. However, keratin resulted to be a suitable biomaterial for APDT, since it has enough resistance to photodegradation and the radical-induced oxidation is not able to induce strong structural changes in the protein. CONCLUSIONS: The results clearly indicate the potential use of these novel photo-active keratin biomatrices in wound dressing and tissue engineering.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160143","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856578","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":"Cholesterol level regulates lectin-like oxidized low-density lipoprotein receptor-1 function","authors":"Sofia Raniolo, Giulia Vindigni, S. Biocca","doi":"10.3233/BSI-160156","DOIUrl":"https://doi.org/10.3233/BSI-160156","url":null,"abstract":"Lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1), the primary receptor for ox-LDL in endothelial cells, is a multi-ligand scavenger receptor that plays a crucial role in the pathogenesis of atherosclerosis and cardiovascular disorders and recently identified as a tumor marker. LOX-1 is naturally present in caveolae/lipid rafts in plasma membranes and disruption of these membrane domains by cholesterol-lowering drugs leads to a spatial disorganization of LOX-1 and a marked loss of specific LOX-1 function in terms of ox-LDL binding and internalization. Moreover, cholesterol depletion triggers the release of LOX-1 in exosomes and enhances shedding of LOX-1 ectodomain. We here provide an overview of the involvement of membrane and circulating cholesterol in LOX-1 function and shedding and its impact on cardiovascular pathologies and cancer. In particular, we consider the available biological and molecular evidence indicating LOX-1 as a potential therapeutic target for atherosclerosis, inflammation processes, myocardial infarction and cholesterol-lowering drugs as specific inhibitors of LOX-1 function.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160156","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856607","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":"Understanding the role of cholesterol in cellular biomechanics and regulation of vesicular trafficking: The power of imaging","authors":"L. O. Andrade","doi":"10.3233/BSI-160157","DOIUrl":"https://doi.org/10.3233/BSI-160157","url":null,"abstract":"Cholesterol is an important component of cell plasma membrane. Due to its chemical composition (long rigid hydrophobic chain and a small polar hydroxyl group), it fits most of its structure into the lipid bilayer, where its steroid rings are in close proximity and attracted to the hydrocarbon chains of neighboring lipids. This gives a condensing effect on the packing of lipids in cell membranes creating cholesterol-enriched regions called membrane rafts, which also congregate a lot of specific proteins. Membrane rafts have been shown to work as platforms involved with signaling in diverse cellular processes, such as immune regulation, cell cycle control, membrane trafficking and fusion events. A series of studies in the last two decades have linked many of these functions with the effects of membrane cholesterol content and rafts integrity on actin cytoskeleton organization, as well as its consequences in cellular biomechanics. This was possible by using microscopy techniques before and after manipulation of cholesterol content from cell plasma membrane, using agents that are able to sequester these molecules, such as cyclodextrins. In this review we’ll give a personal perspective on these studies and how microscopy techniques were important to unravel the effects of cholesterol on actin and cellular mechanics. We will also discuss how actin and cholesterol contributes to control cell secretion and vesicular trafficking.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160157","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856675","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":"Structural properties of paeonol encapsulated liposomes at physiological temperature: Synchrotron small-angle and wide-angle X-ray diffraction studies","authors":"R. Wu, Hai-Yuan Sun, Baoming Zhao, Geng Deng, Zhi‐Wu Yu","doi":"10.3233/BSI-160162","DOIUrl":"https://doi.org/10.3233/BSI-160162","url":null,"abstract":"Structural properties of paeonol-encapsulated liposomes containing cholesterol or stigmasterol at 37°C have been investigated by synchrotron small-angle X-ray scattering (SAXS) and wide-angle X-ray scattering (WAXS) techniques. We compared the structural properties of pure dipalmitoylphosphatidylcholine (DPPC) liposomes, sterol–DPPC liposomes, and those of paeonol–sterol–DPPC liposomes at different molar ratios. Three conclusions can be drawn: First, phase separation occurs in both sterol–DPPC and paeonol–sterol–DPPC liposomes. Second, the incorporation of paeonol molecules into sterol– DPPC liposomes weakens the membrane order. Third, cholesterol has a stronger tendency to interact with DPPC as compared to its counterpart in plant, stigmasterol.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160162","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69857361","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}