@article {44469,
	title = {Enzymatic formation of a skipped methyl-substituted octaprenyl side chain of longestin (KS-505a): involvement of homo-IPP as a common extender unit},
	journal = {Angewandte Chemie},
	volume = {57},
	year = {2018},
	month = {MAY},
	pages = {6629-6632},
	type = {Article},
	abstract = {<p>Longestin (KS-505a), a specific inhibitor of phosphodiesterase, is a meroterpenoid that consists of a unique octacyclic terpene skeleton with branched methyl groups at unusual positions (C1 and C12). The biochemical analysis of Lon23, a methyltransferase involved in the biosynthesis of longestin, demonstrated that methylation of IPP afforded 3Z-3-methyl IPP. This compound as well as IPP was selectively accepted as extender units by Lon22, a geranylgeranyl diphosphate (GGPP) synthase homolog, to yield dimethylated GGPP (dmGGPP). Absolute configuration of dmGGPP was determined to be (4R, 12R) by degradation and chiral GC analysis. These findings led us to propose key steps of the biosynthetic pathway of the unusual homoterpenoid longestin.</p>},
	doi = {10.1002/ange.201802116},
	author = {Taro Ozaki and Shinde, Sandip S. and Gao, Lei and Okuizumi, Ryo and Liu, Chengwei and Ogasawara, Yasushi and Lei, Xiaoguang and Dairi, Tohru and Minami, Atsushi and Oikawa, Hideaki}
}
@article {46615,
	title = {Effect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid beta (1-42) peptide},
	journal = {Biophysical Chemistry},
	volume = {267},
	year = {2020},
	month = {DEC},
	pages = {106480},
	type = {Article},
	abstract = {<p>Imidazolium based IL{\textquoteright}s has gained vast interest in developing biological applications. Oligomerization and fibrillization of amyloid beta (1-42) peptide are mainly responsible for the extra-neuronal deposition of amyloid fibrils in neurodegenerative disorders like Alzheimer{\textquoteright}s disease (AD). Here, we report an effect of tert-BuOH-functional imidazolium ILs on oligomerization and fibrillization of amyloid beta (1-42) Peptide in vitro. In this study, a series of these [alkyl-(t)OHim][OMs] ILs with methyl sulphonate counter anion by varying alkyl chains were used. Among the seven protic ILs, four showed strong binding and inhibition activity for the formation of amyloid beta (1-42) aggregation by using Thioflavin T fluorescence binding assay. The secondary structural analysis of the peptide, pre-incubated with active ILs shows the loss of ordered beta-sheet amyloid structure. The longer alkyl chain ILs showed that an increased in amyloid binding and hence an inhibition effect on amyloid aggregation was enhanced. Thus, we propose that ILs could be presented as potential candidates for therapeutic intervention against Alzheimer{\textquoteright}s disease (AD).</p>
},
	keywords = {Aggregation, Amyloid beta (1-42) peptide, Biofilm inhibitor, Imidazolium ionic liquid},
	issn = {0301-4622},
	doi = {10.1016/j.bpc.2020.106480},
	author = {Said, Madhukar S. and Navale, Govinda R. and Yadav, Ashok and Khonde, Nilesh and Shinde, Sandip S. and Jha, Anjali}
}
