2012
DOI: 10.1016/j.apsusc.2012.02.137
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Immobilization of streptavidin on 4H–SiC for biosensor development

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Cited by 92 publications
(74 citation statements)
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“…Subsequently, after the immobilization of biotin onto the cysteamine SAM, the contact angle decreased to 21.911 ∘ from 46.720 ∘ of the cysteamine SAM. The reason was that the ureido-and tetrahydrothiophene-rings of biotin are more hydrophilic than −NH 2 terminated cysteamine SAM [26]. The contact angle of biotin SAM was smaller than the previously reported one in study [27], and this may be due to the well-organized biotin SAM.…”
Section: Resultscontrasting
confidence: 47%
“…Subsequently, after the immobilization of biotin onto the cysteamine SAM, the contact angle decreased to 21.911 ∘ from 46.720 ∘ of the cysteamine SAM. The reason was that the ureido-and tetrahydrothiophene-rings of biotin are more hydrophilic than −NH 2 terminated cysteamine SAM [26]. The contact angle of biotin SAM was smaller than the previously reported one in study [27], and this may be due to the well-organized biotin SAM.…”
Section: Resultscontrasting
confidence: 47%
“…Streptavidin is one of the most common model proteins used in biosensing studies 64 and its detection is often used as the initial proof-of-concept for new biosensor designs. 28 sensor surface can be given high streptavidin selectivity and affinity by functionalising it with biotin.…”
Section: Streptavidin Biochemistrymentioning
confidence: 99%
“…We present a solution based sequential layer functionalization technique for specific streptavidin (SA) protein immobilization on Si NWs. This functionalization technique combines the protocol for selective SA immobilization to SiC planar surfaces 5 with the "in-suspension" biofunctionalization of NWs developed for the attachment of DNA to Au NWs. 6 An advantage of this technique is the ability to functionalize separate NW batches for the specific attachment of different types of biomolecules.…”
Section: Introductionmentioning
confidence: 99%