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The potential use of glass fiber-reinforced plastic (GFRP) to fabricate single-circuit (SC) and double-circuit (DC) transmission towers was explored herein. Numerical simulations were also done in ANSYS Mechanical software using SOLID186 finite elements. The computations showed that for 110 kV SC and 35 kV and 110 kV DC anchor towers, GFRP structures are not acceptable due to poor stiffness. Different tower configurations with one and two poles made of GFRP and steel–GFRP were modeled. Hybrid steel–GFRP towers exhibited much better stiffness than GFRP ones. Here we advise SC and DC towers with two steel–GFRP columns braced by a metal cage. [ABSTRACT FROM AUTHOR]

Combination antiretroviral therapy (cART) suppresses human immunodeficiency virus-1 (HIV-1) replication but is unable to permanently eradicate HIV-1. Importantly, cART does not target HIV-1 transcription, which is reactivated in latently infected reservoirs, leading to HIV-1 pathogenesis including non-infectious lung, cardiovascular, kidney, and neurodegenerative diseases. To address the limitations of cART and to prevent HIV-1-related pathogenesis, we developed small molecules to target the noncatalytic RVxF-accommodating site of protein phosphatase-1 (PP1) to prevent HIV-1 transcription activation. The PP1 RVxF-accommodating site is critical for the recruitment of regulatory and substrate proteins to PP1. Here, we confirm that our previously developed 1E7-03 compound binds to the PP1 RVxF-accommodating site. Iterative chemical alterations to 1E7-03 furnished a new analogue, HU-1a , with enhanced HIV-1 inhibitory activity and improved metabolic stability compared to 1E7-03 . In a Split NanoBit competition assay, HU-1a primarily bound to the PP1 RVxF-accommodating site. In conclusion, our study identified HU-1a as a promising HIV-1 transcription inhibitor and showed that the PP1 RVxF-accommodating site is a potential drug target for the development of novel HIV-1 transcription inhibitors.