American Chemical Society

The American Chemical Society (ACS) is a scientific society based in the United States that supports scientific inquiry in the field of chemistry. Founded in 1876 at New York University, the ACS currently has more than 155,000 members at all degree levels and in all fields of chemistry, chemical engineering, and related fields. It is one of the world's largest scientific societies by membership. The ACS is a 501(c)(3) non-profit organization and holds a congressional charter under Title 36 of the United States Code. Its headquarters are located in Washington, D.C., and it has a large concentration of staff in Columbus, Ohio. The ACS is a leading source of scientific information through its peer-reviewed scientific journals, national conferences, and the Chemical Abstracts Service. Its publications division produces over 60 scholarly journals including the prestigious Journal of the American Chemical Society, as well as the weekly trade magazine Chemical & Engineering News. The ACS

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This lecture presents the development of catalytic asymmetric reactions in organic chemistry, including important current topics of research in the field.

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Controlling polymer architecture in the thermal hyperbranched polymerization of L-lysine

Harm-Anton Klok, Markus Scholl

Because of the unequal reactivity of the two amine groups of L-lysine hydrochloride, thermal polymerization of this asymmetrical AB2 monomer results in hyperbranched polymers, which contain ?2.5 times more N?-linked linear compared to N?-linked linear structural units. This report discusses the feasibility of three approaches to control polymer architecture during the thermal hyperbranched polymerization of L-lysine hydrochloride. The reactivity of the more reactive ?-NH 2 group was modulated by introducing temporary protective groups that preferentially block the ?-NH2 position. This was achieved by (i) addition of o-vanillin to the polymerization, (ii) copolymerization of N?-benzylidene-L-lysine, and (iii) copolymerization of ?-amino-?-caprolactam. Analysis of the degree of branching (DB) and the average number of branches (ANB) of the obtained polymers did not provide evidence for any significant structural changes. Analysis of the distribution of structural units, in contrast, revealed major structural changes and indicated a rearrangement from N?-linked linear structural units to N ?-linked linear structural units upon addition of o-vanillin and N?-benzylidene-L-lysine. Unlike o-vanillin and N ?-benzylidene-L-lysine, ?-amino-?-caprolactam was found to be rather ineffective in modulating polymer architecture. © 2007 American Chemical Society.

2007

Computational Alanine Scanning Mutagenesis: MM-PBSA vs TI

Marta Andreia Da Silva Perez

Understanding protein-protein association and being able to determine the crucial residues responsible for their association (hot-spots) is a key issue with huge practical applications such as rational drug design and protein engineering. A variety of computational methods exist to detect hot-spots residues, but the development of a fast and accurate quantitative alanine scanning mutagenesis (ASM) continues to be crucial. Using four protein-protein complexes, we have compared a variation of the standard computational ASM protocol developed at our group, based on the Molecular Mechanics/Poisson- Boltzmann Surface Area (MM-PBSA) approach, against Thermodynamic Integration (TI), a well-known and accurate but computationally expensive method. To compare the efficiency and the accuracy of the two methods, we have calculated the protein-protein binding free energy differences upon alanine mutation of interfacial residues (ΔΔGbind). In relation to the experimental ΔΔGbind values, the average error obtained with TI was 1.53 kcal/mol, while the ASM protocol resulted in an average error of 1.18 kcal/mol. The results demonstrate that the much faster ASM protocol gives results at the same level of accuracy as the TI method but at a fraction of the computational time required to run TI. This ASM protocol is therefore a strong and efficient alternative to the systematic evaluation of protein-protein interfaces, involving hundreds of amino acid residues in search of hot-spots. © 2013 American Chemical Society.

2013

Detection of Farnesyltransferase Interface Hot Spots through Computational Alanine Scanning Mutagenesis

Marta Andreia Da Silva Perez

In this study, we present a detailed characterization of the full α/β interface in the farnesyltransferase (FTase) enzyme, an important target in drug design efforts. This characterization is presented in terms of hot spots, warm spots, and null spots and is based on the application of an improved variation of the computational alanine scanning mutagenesis methodology, complemented with extensive solvent-accessible surface area and interfacial hydrogen-bonding analysis. A total of 130 interface amino acid residues were considered in this analysis, a number that represents 16.0% of the total of 814 amino acid residues in the full enzyme. Globally, the results provide important clues on the most important structural and energetic determinants for dimer formation, suggesting several key targets at the subunit interface for the development of new molecules that aim to inhibit FTase activity through blocking the formation of the fully active FTase dimer, yielding useful indications for future drug design efforts. © 2011 American Chemical Society.

2011