คำตอบที่ได้รับเลือกจากเจ้าของกระทู้
ความคิดเห็นที่ 1
ผมใช้ keyword colloidal gold conjugate protocol
ลองดูครับว่าตรงกับความต้องการหรือไม่
สั้นๆคือ hydrophobic interaction
ใช้การลด pH
http://www.protocol-online.org/cgi-bin/prot/view_cache.cgi?ID=455
http://link.springer.com/protocol/10.1385%2F1-59259-213-9%3A331
The ability to conjugate proteins to colloidal gold sols provides a wide variety of probes for electron microscopy. In addition to antibodies, protein A, lectins, enzymes, toxins, and other proteins have all been conjugated to colloidal gold (1–7). The nature of the interaction between the colloidal gold and the protein is poorly understood. Colloidal gold is a negatively charged lyophobic sol. The surface of the particle displays not only electrostatic characteristics, but also hydrophobic properties. In conjugating proteins to a gold sol, the electrostatic interactions must be reduced so that the hydrophobic interactions can prevail. This is accomplished by adjusting the pH of the gold sol to approx 0.5 pH unit higher than the pI of the protein being conjugated. Roth (7) gives a table of optimum pH for a number of commonly used proteins. Once the pH is properly adjusted, the net charge of the protein is zero or slightly negative. This prevents the aggregation of the protein owing to electrostatic attraction while maintaining the hydrophobic interactions and facilitates the conjugation of the protein to the gold.
http://www.cytodiagnostics.com/store/pc/Adsorption-of-Proteins-to-Gold-Nanoparticles-d8.htm
Background
Gold nanoparticle conjugates have been used for a wide range of biological applications including the use as probes in light and electron microscopy. Stable gold nanoparticle conjugates can easily be prepared by passive adsorption due to electrostatic and hydrophobic interactions between the protein and the surface layer of the colloidal gold. This process is maximally achieved at a pH close to the pI of the protein to be conjugated. An important parameter to consider when preparing gold nanoparticle conjugates is the amount of protein bound to the gold colloid. If too little protein is adsorbed to the gold surface, aggregation occurs upon addition of electrolytes present in standard buffers. A titration is therefore performed to determine at which protein concentration saturation and colloidal stability is reached.
ลองดูครับว่าตรงกับความต้องการหรือไม่
สั้นๆคือ hydrophobic interaction
ใช้การลด pH
http://www.protocol-online.org/cgi-bin/prot/view_cache.cgi?ID=455
http://link.springer.com/protocol/10.1385%2F1-59259-213-9%3A331
The ability to conjugate proteins to colloidal gold sols provides a wide variety of probes for electron microscopy. In addition to antibodies, protein A, lectins, enzymes, toxins, and other proteins have all been conjugated to colloidal gold (1–7). The nature of the interaction between the colloidal gold and the protein is poorly understood. Colloidal gold is a negatively charged lyophobic sol. The surface of the particle displays not only electrostatic characteristics, but also hydrophobic properties. In conjugating proteins to a gold sol, the electrostatic interactions must be reduced so that the hydrophobic interactions can prevail. This is accomplished by adjusting the pH of the gold sol to approx 0.5 pH unit higher than the pI of the protein being conjugated. Roth (7) gives a table of optimum pH for a number of commonly used proteins. Once the pH is properly adjusted, the net charge of the protein is zero or slightly negative. This prevents the aggregation of the protein owing to electrostatic attraction while maintaining the hydrophobic interactions and facilitates the conjugation of the protein to the gold.
http://www.cytodiagnostics.com/store/pc/Adsorption-of-Proteins-to-Gold-Nanoparticles-d8.htm
Background
Gold nanoparticle conjugates have been used for a wide range of biological applications including the use as probes in light and electron microscopy. Stable gold nanoparticle conjugates can easily be prepared by passive adsorption due to electrostatic and hydrophobic interactions between the protein and the surface layer of the colloidal gold. This process is maximally achieved at a pH close to the pI of the protein to be conjugated. An important parameter to consider when preparing gold nanoparticle conjugates is the amount of protein bound to the gold colloid. If too little protein is adsorbed to the gold surface, aggregation occurs upon addition of electrolytes present in standard buffers. A titration is therefore performed to determine at which protein concentration saturation and colloidal stability is reached.
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