16-Mercaptohexadecan-1-ol

16-Mercaptohexadecan-1-ol,  16-Mercapto-1-hexadecanol CAS: 114896-32-1 MDL: MFCD03701687

Molecular weight:    274.51 g/mol 

Molecular Formula: C₁₆H₃₄OS

CAS Number:  114896-32-1

Storage: Store at 2-8 C^o, under  dry conditions.

Synonyms:   16-Mercapto-1-hexadecanol, 114896-32-1, 16-sulfanylhexadecan-1-ol, 16-MERCAPTOHEXADECAN-1-OL, 1-Hexadecanol,16-mercapto-, 1-Hexadecanol, 16-mercapto-, 16-mercaptohexadecanol, ACMC-20dt2t, 16-Mercaptohexadecan-l-ol, SCHEMBL944745

Uses:     Synthesis building block, Organic Synthesis, gold and self-assembled monolayers, nanolithography, polyfunctional monolayers, gold colloids

16-Mercaptohexadecan-1-ol is a synthetic specialty chemical useful in the synthesis of pharmaceuticals, nanocomposites, monolayer assemblies and specialty organic chemicals.

Selected references:

 

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8.) Gu, Hongwei, Zhimou Yang, Jinhao Gao, C. K. Chang, and Bing. Xu.   Heterodimers of Nanoparticles: Formation at a Liquid-Liquid Interface and Particle-Specific Surface Modification by Functional Molecules.   Journal of the American Chemical Society 127, no.   (2005): 34–35. https://doi.org/10.1021/ja045220h.

9.) Hermes, Stephan, Felicitas Schroeder, Rolf Chelmowski, Christof Woell, and Roland A. Fischer.   Selective Nucleation and Growth of Metal-Organic Open Framework Thin Films on Patterned COOH/CF3-Terminated Self-Assembled Monolayers on Au(111).   Journal of the American Chemical Society 127, no.   (2005): 13744–45. https://doi.org/10.1021/ja053523l.

10.) Huo, Fengwei, Zijian Zheng, Gengfeng Zheng, Louise R. Giam, Hua Zhang, and Chad A. Mirkin.   Polymer Pen Lithography.   Science (Washington, DC, United States) 321, no.   (2008): 1658–60. https://doi.org/10.1126/science.1162193.

11.) Jung, Linda S., Charles T. Campbell, Timothy M. Chinowsky, Mimi N. Mar, and Sinclair S. Yee.   Quantitative Interpretation of the Response of Surface Plasmon Resonance Sensors to Adsorbed Films.   Langmuir 14, no.   (1998): 5636–48. https://doi.org/10.1021/LA971228B.

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13.) Lahann, Joerg, Samir Mitragotri, Thanh-Nga Tran, Hiroki Kaido, Jagannathan Sundaram, Insung S. Choi, Saskia Hoffer, Gabor A. Somorjai, and Robert. Langer.   A Reversibly Switching Surface.   Science (Washington, DC, United States) 299, no.   (2003): 371–74. https://doi.org/10.1126/science.1078933.

14.) Lee, Ki-Bum, So-Jung Park, Chad A. Mirkin, Jennifer C. Smith, and Milan. Mrksich.   Protein Nanoarrays Generated by Dip-Pen Nanolithography.   Science (Washington, DC, United States) 295, no.   (2002): 1702–5. https://doi.org/10.1126/science.1067172.

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16.) Ostuni, Emanuele, Robert G. Chapman, R. Erik Holmlin, Shuichi Takayama, and George M. Whitesides.   A Survey of Structure-Property Relationships of Surfaces That Resist the Adsorption of Protein.   Langmuir 17, no.   (2001): 5605–20. https://doi.org/10.1021/la010384m.

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18.) Song, Shihua, Rose A. Clark, Edmond F. Bowden, and Michael J. Tarlov.   Characterization of Cytochrome c/Alkanethiolate Structures Prepared by Self-Assembly on Gold.   Journal of Physical Chemistry 97, no.   (1993): 6564–72. https://doi.org/10.1021/j100126a037.

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20.) Xu, Chenjie, Keming Xu, Hongwei Gu, Xiaofen Zhong, Zhihong Guo, Rongkun Zheng, Xixiang Zhang, and Bing. Xu.   Nitrilotriacetic Acid-Modified Magnetic Nanoparticles as a General Agent to Bind Histidine-Tagged Proteins.   Journal of the American Chemical Society 126, no.   (2004): 3392–93. https://doi.org/10.1021/ja031776d.

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