01634nas a2200217   4500008004100000022001400041245011900055210006900174260000800243300001200251490000600263520088000269653001301149653002301162653002101185653001801206653001501224100002301239700002601262856012801288       2018                        eng d  a2365-654900aNovel pentadecyl phenol-tagged L-tryptophan molecules: synthesis, self- assembly and liquid crystalline properties0 aNovel pentadecyl phenoltagged Ltryptophan molecules synthesis se  cJAN  a108-1150 v33 a<p>The paper describes the self-assembly and liquid crystalline properties of pentadecylphenol tagged L-tryptophan molecules having ester and amide functionality. We have synthesized a series of molecules having mono and ditryptophan moieties attached to pentadecylphenol through amide or ester linkage. The fluorescence properties of the Boc-L-tryptophan-pentadecylphenol molecules were measured in methanol and found to aggregate beyond the critical aggregation concentration and self-assembled to give spherical structures. Upon deprotection of Boc group, the amine end group got involved in extended hydrogen bonding and fibril like structures were developed. These molecules also showed liquid crystalline behavior in hydrogen bonding solvents such as benzyl alcohol and showed needle like crystals in tert-butanol, as analyzed by polarized optical light microscopy.</p>10aCardanol10aliquid crystalline10apentadecylphenol10aSelf-assembly10aTryptophan1 aParappurath, Akhil1 aAbraham, Jancy, Nixon  uhttps://library.ncl.res.in/content/novel-pentadecyl-phenol-tagged-l-tryptophan-molecules-synthesis-self-assembly-and-liquid02384nas a2200253   4500008004100000022001400041245011400055210006900169260000800238300001000246490000700256520154000263653002001803653002001823653001301843653001501856653001501871100002101886700002001907700003001927700002201957700002601979856012502005       2022                        eng d  a1075-261700aTryptophan-cardanol fluorescent nanoparticles inhibit alpha-synuclein aggregation and disrupt amyloid fibrils0 aTryptophancardanol fluorescent nanoparticles inhibit alphasynucl  cAPR  ae33740 v283 a<p>
	Protein misfolding and aggregation play a vital role in several human diseases such as Parkinson's, Alzheimer's, and prion diseases. The development of nanoparticles that modulate aggregation could be potential drug candidates for these neurodegenerative disorders. Parkinson's disease pathogenesis is closely associated with the accumulation of alpha-synuclein oligomers and fibrils in the substantia nigra of the brain. This report discusses the interactions of novel tryptophan-cardanol nanoparticles with alpha-synuclein protein monomers and fibrils. These nanoparticles could effectively disrupt alpha-synuclein fibrils and inhibit fibril formation at low concentrations such as 5 mu M. The tryptophan-cardanol nanoparticles inhibit fibril formation from unstructured protein resulting in spherical nanostructures. These nanoparticles could also disassemble amyloid fibrils; the complete disappearance of fibrils was evident after 48 h of incubation with tryptophan-cardanol. The transmission electron microscopy (TEM) micrographs after the incubation did not show any remnants of the peptide aggregates or oligomers. The thioflavin T fluorescence after the disassembly was diminished compared with that of fibrils also supports the inhibitory effect of the nanoparticles. Also, these nanoparticles did not reduce the viability of the SH-SY5Y cells. These findings suggest that the tryptophan-cardanol nanoparticles showed sufficiently high inhibitory activity and may have therapeutic potential for synucleinopathies.</p>
10aalpha-synuclein10aamyloid fibrils10aCardanol10ainhibitors10aTryptophan1 aSunny, Lisni, P.1 aSrikanth, Priya1 aSunitha, Anju, Kunhiraman1 aTembulkar, Niyoti1 aAbraham, Jancy, Nixon  uhttps://library.ncl.res.in/content/tryptophan-cardanol-fluorescent-nanoparticles-inhibit-alpha-synuclein-aggregation-and