@inbook {43302,
	title = {Self-assembly of biohybrid polymers},
	booktitle = {Macromolecular self-assembly},
	year = {2016},
	pages = {193-229},
	publisher = {John Wiley \& Sons, Inc.},
	organization = {John Wiley \& Sons, Inc.},
	chapter = {7},
	address = {New York :},
	abstract = {<p>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.</p>},
	doi = {10.1002/9781118887813.ch7 },
	author = {Kedracki, Dawid and Abraham, Jancy Nixon and Prado, Enora and Nardin, Corinne}
}
@article {44240,
	title = {Interaction of polymers with amyloidogenic peptides},
	journal = {Polymer International},
	volume = {67},
	year = {2018},
	month = {JAN},
	pages = {15-24},
	type = {Article},
	abstract = {<p>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</p>},
	keywords = {amyloid, neurodegenerative diseases, Polymer, protein, Self-assembly},
	issn = {0959-8103},
	doi = {10.1002/pi.5483},
	author = {Abraham, Jancy Nixon and Nardin, Corinne}
}
