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Christina L. L. Chai

Researcher at National University of Singapore

Publications -  189
Citations -  3884

Christina L. L. Chai is an academic researcher from National University of Singapore. The author has contributed to research in topics: Catalysis & Radical polymerization. The author has an hindex of 31, co-authored 184 publications receiving 3470 citations. Previous affiliations of Christina L. L. Chai include Centre for Life & International Council for the Exploration of the Sea.

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Copper-catalyzed oxidative amidation of aldehydes with amine salts: synthesis of primary, secondary, and tertiary amides.

TL;DR: A practical method for the amidation of aldehydes with economic ammonium chloride or amine hydrochloride salts has been developed and has been demonstrated in an efficient synthesis of the antiarrhythmic drug N-acetylprocainamide.
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Conformational selection of inhibitors and substrates by proteolytic enzymes: implications for drug design and polypeptide processing.

TL;DR: Conformational selection explains the resistance of folded/structured regions of proteins to proteolytic degradation, the susceptibility of denatured proteins to processing, and the higher affinity of conformationally constrained 'extended' inhibitors/substrates for proteases.
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Iron-Catalyzed Efficient Synthesis of Amides from Aldehydes and Amine Hydrochloride Salts

TL;DR: The application of this novel amide formation reaction to the synthesis of pharmaceuti- cal compounds has been successfully demonstrated and a wide range of amides have been obtained under mild conditions.
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Iron-Catalysed sp3–sp3 Cross-Coupling Reactions of Unactivated Alkyl Halides with Alkyl Grignard Reagents

TL;DR: In this article, an iron-catalysed sp 3 -sp 3 Kumada coupling with primary and secondary alkyl halides and Grignard reagents has been achieved in low to good yields depending on the nature of the R group.
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Structure−Activity Relationship Studies of Phenanthridine-Based Bcl-XL Inhibitors

TL;DR: The synthesis of phenanthridine-based analogues of the natural products that were used to probe the difference in binding profiles were detailed, which identified the structural motifs required for binding-site specificity as well as inhibitory activity.