Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.11851/749
Title: Mixed-monolayer of N-hydroxysuccinimide-terminated cross-linker and short alkanethiol to improve the efficiency of biomolecule binding for biosensing
Authors: Ataman Sadık, Demet
Eksi-Koçak, Haslet
Ertaş, Gülay
Boyacı, İsmail Hakkı
Mutlu, Mehmet
Keywords: Gold surface modification
Mixed self-assembled monolayer (mSAMs)
Protein immobilization
Surface characterization
Surface plasmon resonance (SPR)
Transducer
Issue Date: 9-Sep-2018
Publisher: John Wiley and Sons Ltd
Source: Ataman Sadık, D., Eksi‐Kocak, H., Ertaş, G., Boyacı, İ. H., & Mutlu, M. (2018). Mixed‐monolayer of N‐hydroxysuccinimide‐terminated cross‐linker and short alkanethiol to improve the efficiency of biomolecule binding for biosensing. Surface and Interface Analysis, 50(9), 866-878.
Abstract: The goal of this study was to use a novel surface chemistry for modifying gold surfaces to decrease the steric hindrance, minimize the nonspecific bindings while providing directed immobilization of proteins for advancing the transducer property and to provide a biosensing platform for surface plasmon resonance (SPR) applications. Mixed self-assembled monolayers (mSAMs) were prepared using 3,3′-Dithiodipropionic acid di (N-hydroxysuccinimide ester) (DSP) and 6-mercapto-1-hexanol (MCH) and the selected model proteins bovine serum albumin (BSA) and lysozyme were tested for binding efficiency. First, binding of these two proteins at constant concentration to different DSP:MCH mSAMs were compared to deduce the best molar ratio for forming mSAM using a continuous flow system coupled to SPR. Coincidently the maximum protein binding DSP:MCH mSAM were the same for both proteins. The change in Response Unit (∆RU) signal due to protein binding between DSP SAM and maximum protein binding DSP:MCH mSAM for lysozyme binding was more in comparison to BSA binding. Second, the effect of BSA and lysozyme concentration on binding efficiency to maximum protein binding DSP:MCH mSAM were compared and discussed. Lysozyme and BSA were shown to reach saturations on the same monolayer at concentrations of 5.7x10−5 and 8.96x10−6 [M] respectively, hence the molar ratio for limit concentrations is 6:1. The DSP SAM, MCH SAM, and DSP:MCH mSAMs where maximum and minimum protein binding occurs were also characterized with XPS and Attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy. Blank gold surface, maximum protein binding DSP:MCH mSAM and BSA immobilized DSP:MCH mSAM on gold surface were also investigated utilizing tapping mode AFM.
URI: https://doi.org/10.1002/sia.6489
https://hdl.handle.net/20.500.11851/749
ISSN: 0142-2421
Appears in Collections:Biyomedikal Mühendisliği Bölümü / Department of Biomedical Engineering
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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