On December 19, 2014, Khoury, George A.; Smadbeck, James; Tamamis, Phanourios; Vandris, Andrew C.; Kieslich, Chris A.; Floudas, Christodoulos A. published an article.Synthetic Route of 32462-30-9 The title of the article was Forcefield_NCAA: Ab Initio Charge Parameters to Aid in the Discovery and Design of Therapeutic Proteins and Peptides with Unnatural Amino Acids and Their Application to Complement Inhibitors of the Compstatin Family. And the article contained the following:
We describe the development and testing of ab initio derived, AMBER ff03 compatible charge parameters for a large library of 147 noncanonical amino acids including β- and N-methylated amino acids for use in applications such as protein structure prediction and de novo protein design. The charge parameter derivation was performed using the RESP fitting approach. Studies were performed assessing the suitability of the derived charge parameters in discriminating the activity/inactivity between 63 analogs of the complement inhibitor Compstatin on the basis of previously published exptl. IC50 data and a screening procedure involving short simulations and binding free energy calculations We found that both the approx. binding affinity (K*) and the binding free energy calculated through MM-GBSA are capable of discriminating between active and inactive Compstatin analogs, with MM-GBSA performing significantly better. Key interactions between the most potent Compstatin analog that contains a noncanonical amino acid are presented and compared to the most potent analog containing only natural amino acids and native Compstatin. We make the derived parameters and an associated web interface that is capable of performing modifications on proteins using Forcefield_NCAA and outputting AMBER-ready topol. and parameter files freely available for academic use at http://selene.princeton.edu/FFNCAA. The forcefield allows one to incorporate these customized amino acids into design applications with control over size, van der Waals, and electrostatic interactions. The experimental process involved the reaction of H-Phg(4-OH)-OH(cas: 32462-30-9).Synthetic Route of 32462-30-9
The Article related to compstatin analog noncanonical amino acid complement inhibitor drug design, mol dynamics simulation unnatural amino acid therapeutic protein peptide, amber topol noncanonical amino acid pharmacophore compstatin analog design, amber partial charges, compstatin, complement, inhibitors, molecular dynamics, noncanonical amino acids, unnatural amino acids and other aspects.Synthetic Route of 32462-30-9
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