23082-32-8Relevant academic research and scientific papers
Design and synthesis of Hsp90 inhibitors: Exploring the SAR of Sansalvamide A derivatives
Sellers, Robert P.,Alexander, Leslie D.,Johnson, Victoria A.,Lin, Chun-Chieh,Savage, Jeremiah,Corral, Ricardo,Moss, Jason,Slugocki, Tim S.,Singh, Erinprit K.,Davis, Melinda R.,Ravula, Suchitra,Spicer, Jamie E.,Oelrich, Jenna L.,Thornquist, Andrea,Pan, Chung-Mao,McAlpine, Shelli R.
experimental part, p. 6822 - 6856 (2010/10/18)
Utilizing the structure-activity relationship we have developed during the synthesis of the first two generations and mechanism of action studies that point to the interaction of these molecules with the key oncogenic protein Hsp90, we report here the design of 32 new Sansalvamide A derivatives and their synthesis. Our new structures, designed from previously reported potent compounds, were tested for cytotoxicity on the HCT116 colon cancer cell line, and their binding to the biological target was analyzed using computational studies involving blind docking of derivatives using Autodock. Further, we show new evidence that our molecules bind directly to Hsp90 and modulate Hsp90's binding with client proteins. Finally, we demonstrate that we have integrated good ADME properties into a new derivative.
A rapid and efficient synthesis of β-casomorphin employing Boc-amino acids and 9-fluorenylmethyl chloroformate as a coupling agent
Babu, V.V. Suresh,Tantry
, p. 2708 - 2712 (2007/10/03)
The synthesis of β-casomorphin H-Tyr-Pro-Phe-Pro-Gly-OH employing Boc group for Nα-protection and 9-fluorenylmethyl chloroformate (Fmoc-Cl) for the formation of peptide bond is described. The protocol employing Fmoc-Cl as coupling reagent is found to be simple, efficient and rapid. All the intermediate peptides as well as the final protected peptide Boc-Tyr( iBu)-Pro-Phe-Pro-Gly-OMe have been isolated and fully characterized. They have been obtained in good yield and with high purity.
Conformationally constrained [p-(ω-aminoalkyl)phenacetyl]-L-seryl-L- lysyl dipeptide amides as potent peptidomimetic inhibitors of Candida albicans and human myristoyl-CoA:protein N-myristoyl transferase
Nagarajan, Srinivasan R.,Devadas, Balekudru,Zupec, Mark E.,Freeman, Sandra K.,Brown, David L.,Lu, Hwang-Fun,Mehta, Pramod P.,Kishore, Nandini S.,McWherter, Charles A.,Getman, Daniel P.,Gordon, Jeffrey I.,Sikorski, James A.
, p. 1422 - 1438 (2007/10/03)
MyristoylCoA:protein N-myristoyltransferase (NMT) covalently attaches the 14-carbon saturated fatty acid myristate, via an amide bond, to the N- terminal glycine residues of a variety of cellular proteins. Genetic studies have shown that NMT is essential
