Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
Inducing the bio-functionalization in noble metal nanoparticles like gold, silver, zinc is very important to accomplish their biocompatibility in biological activities. These metal nanoparticles are being rigorously used in bio-sensing tools keeping their remarkable properties in mind. Amongst the serum albumins, the most ample proteins in plasma are bovine serum albumin and human serum albumin. A broad variety of physiological functions of bovine serum albumin has made it a model protein for bio-functionalization. In the present study, ZnO/Ag nanoparticles were synthesized and characterized by SEM and XRD techniques and the interaction between bovine serum albumin and ZnO/Ag nanoparticles was evaluated by employing ultra-violet, steady state fluorescence, circular dichroism and FTIR spectroscopic techniques. Upon the excitation of bovine serum albumin, ZnO/Ag nanoparticles appreciably reduced the intrinsic fluorescence intensity of bovine serum albumin. The number of binding locations and apparent binding constants at different temperatures were calculated by the fluorescence quenching method. Static mechanism of quenching and conformational modifications in bovine serum albumin were also found.Communicated by Ramaswamy H. Sarma.
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Source |
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http://dx.doi.org/10.1080/07391102.2021.2006788 | DOI Listing |
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