01636nas a2200157 4500008004100000245004000041210003900081260004000120300001200160520115100172100002001323700002601343700001701369700002001386856007201406 2016 eng d00aSelf-assembly of biohybrid polymers0 aSelfassembly of biohybrid polymers aNew York :bJohn Wiley & Sons, Inc. a193-2293 a

Self-assembly is considered to be the process through which building blocks spontaneously organize into well-defined frequently functional structures. The tailoring of properties of such structures has drawn attention in various fields, in particular, in enzymatic cascade reactions, drug delivery, amphiphilic copolymer nanocontainers, and nanoreactors. Polymer-DNA hybrid self-assemblies, in addition to responsiveness to ionic strength, are sensitive to hybridization, which renders the establishment of a theoretical framework challenging when both specific hydrogen bonding between complementary sequences and association are to be taken into consideration. Numerous various highly characterized self-assemblies are recognized to organize through nucleation dependent polymerization, including microtubule formation, sickle-cell fibril formation, flagellum assembly, among others. Interpolyelectrolyte complexes (IPECs) have attracted attention due to the large number of emerging and potential applications. Environmental factors such as the medium also play a role in the complex formation process, especially pH and ionic strength.

1 aKedracki, Dawid1 aAbraham, Jancy, Nixon1 aPrado, Enora1 aNardin, Corinne uhttps://library.ncl.res.in/content/self-assembly-biohybrid-polymers01835nas a2200217 4500008004100000022001400041245005600055210005600111260000800167300001000175490000700185520121100192653001201403653003101415653001201446653001201458653001801470100002601488700002001514856008301534 2018 eng d a0959-810300aInteraction of polymers with amyloidogenic peptides0 aInteraction of polymers with amyloidogenic peptides cJAN a15-240 v673 a

With this review, the aim was to gather recent representative publications which describe the interaction of polymers with amyloidogenic peptides/proteins. When functional, these take part in for instance bacterial adhesion and biofilm formation. However, several of the peptides/proteins have been identified in various diseases. One of the current approaches to discover a cure against these relies on therapeutics which either prevent or accelerate peptide/protein aggregation and/or clear readily formed aggregates. Owing to the common interest of scientists from all disciplines to identify a cure against the diseases of public health concern, there are overwhelming numbers of publications dealing with these two approaches. Since amyloid aggregation could be regarded as a nucleated polymerization, which is an established mechanism of polymer self-assembly, we recently tackled the issue of amyloid aggregation using the theories and methods established in polymer science. In this review, we hence focus on gathering relevant and recent publications which describe the role of polymers in modulating the aggregation of amyloidogenic peptides/proteins. (c) 2017 Society of Chemical Industry

10aamyloid10aneurodegenerative diseases10aPolymer10aprotein10aSelf-assembly1 aAbraham, Jancy, Nixon1 aNardin, Corinne uhttps://library.ncl.res.in/content/interaction-polymers-amyloidogenic-peptides01634nas 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

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.

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-liquid02108nas a2200169 4500008004100000022001400041245013300055210006900188260000900257300001400266490000700280520145700287100001901744700001801763700002601781856013101807 2020 eng d a1744-683X00aSelf-assembly of novel Fmoc-cardanol compounds into hydrogels - analysis based on rheological, structural and thermal properties0 aSelfassembly of novel Fmoccardanol compounds into hydrogels anal cJUL  a6294-63030 v163 a

Hydrogels of low molecular weight molecules are particularly appealing for various biomedical applications such as drug delivery, tissue engineering, and antitumor therapy due to their excellent biocompatibility, biodegradability, and easy availability. Fmoc-peptide hydrogels form an essential category of these hydrogels. Herein we report a new class of Fmoc hydrogels in which cardanol (3-pentadecyl phenol (PDP)) is covalently linked with fluorenylmethyloxycarbonyl group. Cardanol is a plant-based renewable raw material, readily obtained from Cashew Nut Shell Liquid (CNSL). The long aliphatic chain of pentadecyl phenol helps in bringing a structural incompatibility and generates different nanostructures such as nanospheres, nanotapes, and nanofibers depending on Fmoc substitution and the solvents used. Stable hydrogels were formed from Fmoc-PDP in DMSO/H2O, and the critical aggregation concentration (CAC) and critical gelation concentration (CGC) were determined. The role of non-covalent forces such as hydrogen-bonding, hydrophobicity, and pi-pi stacking interactions in governing self-assembly to hydrogel formation was studied for Fmoc, DiFmoc and Boc groups attached to PDP. The thermal properties were analyzed, and smectic and nematic phases were identified for the molecules depending on the substitutions involved. Overall the study supports the mechanisms of aggregation and gelation in novel Fmoc-cardanol derivatives.

1 aKadeeja, Aliya1 aJoseph, Seena1 aAbraham, Jancy, Nixon uhttps://library.ncl.res.in/content/self-assembly-novel-fmoc-cardanol-compounds-hydrogels-analysis-based-rheological-structural02384nas 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

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.

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