Kiyoshi Fukuhara, Ikuo Nakanishi, Hiromu Ito, Wakana Shimizu, Yoshimi Shoji, Kei Ohkubo, Masao Morita, Sakurako Okada, Akiko Ohno
Oxidative stress is a major driver of chronic disease, making natural polyphenols attractive scaffolds for modulating inflammation, proteostasis, and cell fate. However, green-tea catechins possess a twisted, conformationally flexible flavan-3-ol framework that limits π-conjugation, phenoxyl-radical stabilization, and productive interactions with biological targets. This review presents a structure-based framework in which conformational planarization serves as a strategy for functional amplification. Preorganization of the A/C-B inter-ring bond into a nearly coplanar arrangement reduces the conformational entropy penalty (-TΔS) upon binding or reaction while extending conjugation, strengthening π-π interactions, and facilitating redox reactions. This review highlights planarized catechin (PCat) architectures, including PCat-DTPA (a lesion-activated metal-responsive antioxidant), PCat-TrOH (a self-regenerating antioxidant network), procyanidin B3-PCat hybrids, and a planar silybin analog, illustrating how planarization and multivalent recognition enhance ROS regulation, inhibit amyloid-β aggregation and neurotoxicity, and suppress cancer cell phenotypes. Collectively, these studies establish PCat as a modular platform for the mechanism-informed design of disease-tailored phenolic antioxidants.