Highly selective detection of l-Phenylalanine by molecularly imprinted polymers coated Au nanoparticles via surface-enhanced Raman scattering
Molecularly imprinted film coated gold nanoprticles (MIP-AuNPs) were employed as surface-enhanced Raman scattering (SERS) substrate for sensitive and selective recognition and quantification of l-Phenylalanine (L-Phe). The MIP was in-situ formed on the AuNPs by sol-gel technique using L-Phe as the t...
Saved in:
Published in | Talanta (Oxford) Vol. 211; p. 120745 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.05.2020
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Molecularly imprinted film coated gold nanoprticles (MIP-AuNPs) were employed as surface-enhanced Raman scattering (SERS) substrate for sensitive and selective recognition and quantification of l-Phenylalanine (L-Phe). The MIP was in-situ formed on the AuNPs by sol-gel technique using L-Phe as the template molecule, tetraethyl orthosilicate as the crosslinker and phenyltrimethoxysilane as the functional monomer. The efficient removal of template was achieved by ultrasonic treatment. The as-prepared MIP-AuNPs sensor showed a good linear relationship with the concentration of L-Phe in the range of 1.0 × 10−8–1.0 × 10−4 mol L−1 with a limit of detection as low as 1.0 nmol L−1. The sensor also showed an excellent selectivity as L-Phe can be determined in the presence of other amino acid analogues, D-Phe and bovine serum. The stability of the MIP-AuNPs was manifested by the low deviation (RSD = 3.7%) for 40 days subsequent measurements.
[Display omitted]
•The MIPs functionalized AuNPs were used as a SERS substrate for sensitive and selective detection of l-Phenylalanine.•The efficient removal of template was achieved by ultrasonic treatment.•The thickness of MIPs on AuNPs was tuned in-situ by controlling the amount of precursors to achieve best SERS performance.•l-Phenylalanine was successfully detected with the probe in the coexistence of protein. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0039-9140 1873-3573 |
DOI: | 10.1016/j.talanta.2020.120745 |