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: 3122
Function: getPubMedXML
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
We describe the site-specific and chemoselective immobilization of peptides on hydrogen-terminated silicon nanowires (SiNWs) using native chemical ligation (NCL) (i.e., the reaction of a thioester group with a cysteine moiety to give a stable amide bond). The SiNWs investigated in this work were grown via a vapor-liquid-solid mechanism and functionalized with a thioester moiety. The immobilization of the peptides on the SiNWs was demonstrated by synthesizing peptides with an N-terminal cysteine residue and labeled with tetramethylrhodamine or trifluoromethyl groups that were detected by fluorescence and X-ray photoelectron spectroscopy, respectively. The peptides labeled with tetramethylrhodamine or trifluoromethyl groups for fluorescence or X-ray photoelectron spectroscopy (XPS) detection studies were synthesized with an N-terminal cysteine residue. N-Terminal seryl peptides and carboxy-terminated SiNWs were used as controls to demonstrate the chemoselectivity of the peptide immobilization.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1021/la3030217 | DOI Listing |
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