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Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana: a multispectroscopic approach
This study describes the eco‐friendly, low‐cost and room‐temperature synthesis of gold nanoparticles from Musa balbisiana leaf extract, which acts as both reducing and stabilizing agent, and characterized by ultraviolet−visible (UV–vis) light spectroscopy, fourier transform infrared (FTIR) spectrosc...
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| Published in: | Luminescence (Chichester, England) England), 2019-09, Vol.34 (6), p.563-575 |
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| cited_by | cdi_FETCH-LOGICAL-c3499-1f134614508bd07a7489c587ee40a553bc77411648a61bffb6f98d088e9d09ee3 |
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| cites | cdi_FETCH-LOGICAL-c3499-1f134614508bd07a7489c587ee40a553bc77411648a61bffb6f98d088e9d09ee3 |
| container_end_page | 575 |
| container_issue | 6 |
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| container_title | Luminescence (Chichester, England) |
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| creator | Maji, Anukul Beg, Maidul Das, Somnath Sahoo, Nandan Kumar Jha, Pradeep K. Islam, Md. Maidul Hossain, Maidul |
| description | This study describes the eco‐friendly, low‐cost and room‐temperature synthesis of gold nanoparticles from Musa balbisiana leaf extract, which acts as both reducing and stabilizing agent, and characterized by ultraviolet−visible (UV–vis) light spectroscopy, fourier transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FE‐SEM), analytical transmission electron microscopy (TEM), energy‐dispersive X‐ray spectroscopy (EDAX) and dynamic light scattering (DLS) instruments. These nanoparticles showed an average diameter of 33.83 ± 3.39 nm, which was confirmed from the size distribution histogram. The bactericidal activity of these nanoparticles was confirmed using bacteria Escherichia coli and Staphylococcus aureus at 1 and 2 nM minimum inhibitory concentrations, respectively. The interaction between nanoparticles and human serum albumin (HSA) was investigated, as this plays significant roles in biological systems. The nature of interaction, binding parameters and structural variation of HSA in the presence of these nanoparticles have been evaluated using several useful spectroscopic approaches such as UV–vis, FTIR, time‐resolved and steady‐state fluorescence, and circular dichroism in addition to the measurement of zeta potential. This interaction study revealed that static quenching occurs in this process with minimal alteration in the secondary structure, but the native structure of HSA remained unaltered. The binding constant and thermodynamic parameters of this interaction process were also evaluated. |
| doi_str_mv | 10.1002/bio.3639 |
| format | article |
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Maidul ; Hossain, Maidul</creator><creatorcontrib>Maji, Anukul ; Beg, Maidul ; Das, Somnath ; Sahoo, Nandan Kumar ; Jha, Pradeep K. ; Islam, Md. Maidul ; Hossain, Maidul</creatorcontrib><description>This study describes the eco‐friendly, low‐cost and room‐temperature synthesis of gold nanoparticles from Musa balbisiana leaf extract, which acts as both reducing and stabilizing agent, and characterized by ultraviolet−visible (UV–vis) light spectroscopy, fourier transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FE‐SEM), analytical transmission electron microscopy (TEM), energy‐dispersive X‐ray spectroscopy (EDAX) and dynamic light scattering (DLS) instruments. These nanoparticles showed an average diameter of 33.83 ± 3.39 nm, which was confirmed from the size distribution histogram. The bactericidal activity of these nanoparticles was confirmed using bacteria Escherichia coli and Staphylococcus aureus at 1 and 2 nM minimum inhibitory concentrations, respectively. The interaction between nanoparticles and human serum albumin (HSA) was investigated, as this plays significant roles in biological systems. The nature of interaction, binding parameters and structural variation of HSA in the presence of these nanoparticles have been evaluated using several useful spectroscopic approaches such as UV–vis, FTIR, time‐resolved and steady‐state fluorescence, and circular dichroism in addition to the measurement of zeta potential. This interaction study revealed that static quenching occurs in this process with minimal alteration in the secondary structure, but the native structure of HSA remained unaltered. The binding constant and thermodynamic parameters of this interaction process were also evaluated.</description><identifier>ISSN: 1522-7235</identifier><identifier>EISSN: 1522-7243</identifier><identifier>DOI: 10.1002/bio.3639</identifier><identifier>PMID: 31044511</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Albumin ; Albumins ; Analytical methods ; Anti-Bacterial Agents - chemical synthesis ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Bacteria ; Bactericidal activity ; bactericidal property ; Binding ; Circular Dichroism ; Dichroism ; E coli ; Electron microscopy ; Emission analysis ; Energy transmission ; Escherichia coli - drug effects ; Field emission microscopy ; Field emission spectroscopy ; Fluorescence ; fluorescence studies ; Fourier transforms ; Gold ; Gold - chemistry ; Gold - pharmacology ; Histograms ; Human serum albumin ; Humans ; Infrared analysis ; Infrared spectroscopy ; Instruments ; Interaction parameters ; Leaves ; Light scattering ; Mathematical analysis ; Metal Nanoparticles - chemistry ; MGNs synthesis ; MGNs–HSA conjugate ; Microscopy ; Musa - chemistry ; Musa balbisiana ; Nanoparticles ; Parameters ; Particle Size ; Photon correlation spectroscopy ; Plant extracts ; Plant Extracts - chemistry ; Plant Leaves - chemistry ; Process parameters ; Protein Binding ; Protein structure ; Scanning electron microscopy ; Secondary structure ; Serum ; Serum albumin ; Serum Albumin, Human - chemistry ; Size distribution ; Spectrophotometry, Ultraviolet ; Spectroscopy ; Spectroscopy, Fourier Transform Infrared ; Spectrum analysis ; Stabilizers (agents) ; Stabilizing ; Staphylococcus aureus - drug effects ; Transmission electron microscopy ; Ultraviolet radiation ; Zeta potential</subject><ispartof>Luminescence (Chichester, England), 2019-09, Vol.34 (6), p.563-575</ispartof><rights>2019 John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3499-1f134614508bd07a7489c587ee40a553bc77411648a61bffb6f98d088e9d09ee3</citedby><cites>FETCH-LOGICAL-c3499-1f134614508bd07a7489c587ee40a553bc77411648a61bffb6f98d088e9d09ee3</cites><orcidid>0000-0003-1408-2273</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31044511$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Maji, Anukul</creatorcontrib><creatorcontrib>Beg, Maidul</creatorcontrib><creatorcontrib>Das, Somnath</creatorcontrib><creatorcontrib>Sahoo, Nandan Kumar</creatorcontrib><creatorcontrib>Jha, Pradeep K.</creatorcontrib><creatorcontrib>Islam, Md. Maidul</creatorcontrib><creatorcontrib>Hossain, Maidul</creatorcontrib><title>Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana: a multispectroscopic approach</title><title>Luminescence (Chichester, England)</title><addtitle>Luminescence</addtitle><description>This study describes the eco‐friendly, low‐cost and room‐temperature synthesis of gold nanoparticles from Musa balbisiana leaf extract, which acts as both reducing and stabilizing agent, and characterized by ultraviolet−visible (UV–vis) light spectroscopy, fourier transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FE‐SEM), analytical transmission electron microscopy (TEM), energy‐dispersive X‐ray spectroscopy (EDAX) and dynamic light scattering (DLS) instruments. These nanoparticles showed an average diameter of 33.83 ± 3.39 nm, which was confirmed from the size distribution histogram. The bactericidal activity of these nanoparticles was confirmed using bacteria Escherichia coli and Staphylococcus aureus at 1 and 2 nM minimum inhibitory concentrations, respectively. The interaction between nanoparticles and human serum albumin (HSA) was investigated, as this plays significant roles in biological systems. The nature of interaction, binding parameters and structural variation of HSA in the presence of these nanoparticles have been evaluated using several useful spectroscopic approaches such as UV–vis, FTIR, time‐resolved and steady‐state fluorescence, and circular dichroism in addition to the measurement of zeta potential. This interaction study revealed that static quenching occurs in this process with minimal alteration in the secondary structure, but the native structure of HSA remained unaltered. The binding constant and thermodynamic parameters of this interaction process were also evaluated.</description><subject>Albumin</subject><subject>Albumins</subject><subject>Analytical methods</subject><subject>Anti-Bacterial Agents - chemical synthesis</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Bacteria</subject><subject>Bactericidal activity</subject><subject>bactericidal property</subject><subject>Binding</subject><subject>Circular Dichroism</subject><subject>Dichroism</subject><subject>E coli</subject><subject>Electron microscopy</subject><subject>Emission analysis</subject><subject>Energy transmission</subject><subject>Escherichia coli - drug effects</subject><subject>Field emission microscopy</subject><subject>Field emission spectroscopy</subject><subject>Fluorescence</subject><subject>fluorescence studies</subject><subject>Fourier transforms</subject><subject>Gold</subject><subject>Gold - chemistry</subject><subject>Gold - pharmacology</subject><subject>Histograms</subject><subject>Human serum albumin</subject><subject>Humans</subject><subject>Infrared analysis</subject><subject>Infrared spectroscopy</subject><subject>Instruments</subject><subject>Interaction parameters</subject><subject>Leaves</subject><subject>Light scattering</subject><subject>Mathematical analysis</subject><subject>Metal Nanoparticles - chemistry</subject><subject>MGNs synthesis</subject><subject>MGNs–HSA conjugate</subject><subject>Microscopy</subject><subject>Musa - chemistry</subject><subject>Musa balbisiana</subject><subject>Nanoparticles</subject><subject>Parameters</subject><subject>Particle Size</subject><subject>Photon correlation spectroscopy</subject><subject>Plant extracts</subject><subject>Plant Extracts - chemistry</subject><subject>Plant Leaves - chemistry</subject><subject>Process parameters</subject><subject>Protein Binding</subject><subject>Protein structure</subject><subject>Scanning electron microscopy</subject><subject>Secondary structure</subject><subject>Serum</subject><subject>Serum albumin</subject><subject>Serum Albumin, Human - chemistry</subject><subject>Size distribution</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spectroscopy</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Spectrum analysis</subject><subject>Stabilizers (agents)</subject><subject>Stabilizing</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Transmission electron microscopy</subject><subject>Ultraviolet radiation</subject><subject>Zeta potential</subject><issn>1522-7235</issn><issn>1522-7243</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNp1kc9OFTEUhydGIogmPoFp4sbNQDttZ6buhIiSYNjoetJpT7klnXbsn8D1hXxNegUhIXHV0-Q732nPr2neEXxEMO6OZxuOaE_Fi-aA8K5rh47Rl4815fvN65SuMcZ934tXzT4lmDFOyEHz58R6bf0Vsj5DlCrb4FHKRW9RLTZlkfUKsSxIurks1qMbmzdoriREq6yWDl0Fp5GXPqwyZqscJJS2Pm8g2d-gkYmhdiMH0iC4zbshKBj0vSRZPW62yUovP1VkKS7btILKMSQVVquQXNcYpNq8afaMdAnePpyHzc-zLz9Ov7UXl1_PTz9ftIoyIVpiCGU9YRyPs8aDHNgoFB8HAIYl53RWw8AI6dkoezIbM_dGjBqPIwiNBQA9bD7ee-vYXwVSnhabFDgnPYSSpq4joxAD46KiH56h16FEX19XqZGJumBOnoSq_ilFMNMa7SLjdiJ42oU31fCmXXgVff8gLPMC-hH8l1YF2nvgxjrY_lc0nZxf_hXeARSnpek</recordid><startdate>201909</startdate><enddate>201909</enddate><creator>Maji, Anukul</creator><creator>Beg, Maidul</creator><creator>Das, Somnath</creator><creator>Sahoo, Nandan Kumar</creator><creator>Jha, Pradeep K.</creator><creator>Islam, Md. Maidul</creator><creator>Hossain, Maidul</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QP</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>7U7</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H95</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L.G</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-1408-2273</orcidid></search><sort><creationdate>201909</creationdate><title>Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana: a multispectroscopic approach</title><author>Maji, Anukul ; Beg, Maidul ; Das, Somnath ; Sahoo, Nandan Kumar ; Jha, Pradeep K. ; Islam, Md. Maidul ; Hossain, Maidul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3499-1f134614508bd07a7489c587ee40a553bc77411648a61bffb6f98d088e9d09ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Albumin</topic><topic>Albumins</topic><topic>Analytical methods</topic><topic>Anti-Bacterial Agents - chemical synthesis</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Bacteria</topic><topic>Bactericidal activity</topic><topic>bactericidal property</topic><topic>Binding</topic><topic>Circular Dichroism</topic><topic>Dichroism</topic><topic>E coli</topic><topic>Electron microscopy</topic><topic>Emission analysis</topic><topic>Energy transmission</topic><topic>Escherichia coli - drug effects</topic><topic>Field emission microscopy</topic><topic>Field emission spectroscopy</topic><topic>Fluorescence</topic><topic>fluorescence studies</topic><topic>Fourier transforms</topic><topic>Gold</topic><topic>Gold - chemistry</topic><topic>Gold - pharmacology</topic><topic>Histograms</topic><topic>Human serum albumin</topic><topic>Humans</topic><topic>Infrared analysis</topic><topic>Infrared spectroscopy</topic><topic>Instruments</topic><topic>Interaction parameters</topic><topic>Leaves</topic><topic>Light scattering</topic><topic>Mathematical analysis</topic><topic>Metal Nanoparticles - chemistry</topic><topic>MGNs synthesis</topic><topic>MGNs–HSA conjugate</topic><topic>Microscopy</topic><topic>Musa - chemistry</topic><topic>Musa balbisiana</topic><topic>Nanoparticles</topic><topic>Parameters</topic><topic>Particle Size</topic><topic>Photon correlation spectroscopy</topic><topic>Plant extracts</topic><topic>Plant Extracts - chemistry</topic><topic>Plant Leaves - chemistry</topic><topic>Process parameters</topic><topic>Protein Binding</topic><topic>Protein structure</topic><topic>Scanning electron microscopy</topic><topic>Secondary structure</topic><topic>Serum</topic><topic>Serum albumin</topic><topic>Serum Albumin, Human - chemistry</topic><topic>Size distribution</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Spectroscopy</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Spectrum analysis</topic><topic>Stabilizers (agents)</topic><topic>Stabilizing</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Transmission electron microscopy</topic><topic>Ultraviolet radiation</topic><topic>Zeta potential</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maji, Anukul</creatorcontrib><creatorcontrib>Beg, Maidul</creatorcontrib><creatorcontrib>Das, Somnath</creatorcontrib><creatorcontrib>Sahoo, Nandan Kumar</creatorcontrib><creatorcontrib>Jha, Pradeep K.</creatorcontrib><creatorcontrib>Islam, Md. Maidul</creatorcontrib><creatorcontrib>Hossain, Maidul</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Luminescence (Chichester, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maji, Anukul</au><au>Beg, Maidul</au><au>Das, Somnath</au><au>Sahoo, Nandan Kumar</au><au>Jha, Pradeep K.</au><au>Islam, Md. Maidul</au><au>Hossain, Maidul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana: a multispectroscopic approach</atitle><jtitle>Luminescence (Chichester, England)</jtitle><addtitle>Luminescence</addtitle><date>2019-09</date><risdate>2019</risdate><volume>34</volume><issue>6</issue><spage>563</spage><epage>575</epage><pages>563-575</pages><issn>1522-7235</issn><eissn>1522-7243</eissn><abstract>This study describes the eco‐friendly, low‐cost and room‐temperature synthesis of gold nanoparticles from Musa balbisiana leaf extract, which acts as both reducing and stabilizing agent, and characterized by ultraviolet−visible (UV–vis) light spectroscopy, fourier transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FE‐SEM), analytical transmission electron microscopy (TEM), energy‐dispersive X‐ray spectroscopy (EDAX) and dynamic light scattering (DLS) instruments. These nanoparticles showed an average diameter of 33.83 ± 3.39 nm, which was confirmed from the size distribution histogram. The bactericidal activity of these nanoparticles was confirmed using bacteria Escherichia coli and Staphylococcus aureus at 1 and 2 nM minimum inhibitory concentrations, respectively. The interaction between nanoparticles and human serum albumin (HSA) was investigated, as this plays significant roles in biological systems. The nature of interaction, binding parameters and structural variation of HSA in the presence of these nanoparticles have been evaluated using several useful spectroscopic approaches such as UV–vis, FTIR, time‐resolved and steady‐state fluorescence, and circular dichroism in addition to the measurement of zeta potential. This interaction study revealed that static quenching occurs in this process with minimal alteration in the secondary structure, but the native structure of HSA remained unaltered. The binding constant and thermodynamic parameters of this interaction process were also evaluated.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>31044511</pmid><doi>10.1002/bio.3639</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0003-1408-2273</orcidid></addata></record> |
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| ispartof | Luminescence (Chichester, England), 2019-09, Vol.34 (6), p.563-575 |
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| language | eng |
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| subjects | Albumin Albumins Analytical methods Anti-Bacterial Agents - chemical synthesis Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Bacteria Bactericidal activity bactericidal property Binding Circular Dichroism Dichroism E coli Electron microscopy Emission analysis Energy transmission Escherichia coli - drug effects Field emission microscopy Field emission spectroscopy Fluorescence fluorescence studies Fourier transforms Gold Gold - chemistry Gold - pharmacology Histograms Human serum albumin Humans Infrared analysis Infrared spectroscopy Instruments Interaction parameters Leaves Light scattering Mathematical analysis Metal Nanoparticles - chemistry MGNs synthesis MGNs–HSA conjugate Microscopy Musa - chemistry Musa balbisiana Nanoparticles Parameters Particle Size Photon correlation spectroscopy Plant extracts Plant Extracts - chemistry Plant Leaves - chemistry Process parameters Protein Binding Protein structure Scanning electron microscopy Secondary structure Serum Serum albumin Serum Albumin, Human - chemistry Size distribution Spectrophotometry, Ultraviolet Spectroscopy Spectroscopy, Fourier Transform Infrared Spectrum analysis Stabilizers (agents) Stabilizing Staphylococcus aureus - drug effects Transmission electron microscopy Ultraviolet radiation Zeta potential |
| title | Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana: a multispectroscopic approach |
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