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dc.contributor.author
Pohl, Gábor
dc.contributor.author
Jákli, Imre
dc.contributor.author
Csizmadia, Imre G.
dc.contributor.author
Papp, Dóra
dc.contributor.author
Garibotto, Francisco Matías
dc.contributor.author
Perczel, András
dc.date.available
2017-03-30T14:54:33Z
dc.date.issued
2012-01-28
dc.identifier.citation
Pohl, Gábor; Jákli, Imre; Csizmadia, Imre G.; Papp, Dóra; Garibotto, Francisco Matías; et al.; The role of entropy in initializing the aggregation of peptides: a first principle study on oligopeptide oligomerization; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 14; 4; 28-1-2012; 1507-1516
dc.identifier.issn
1463-9076
dc.identifier.uri
http://hdl.handle.net/11336/14506
dc.description.abstract
The initiation and progression of Alzheimer's disease is coupled to the oligo- and polymerization of amyloid peptides in the brain. Amyloid like aggregates of protein domains were found practically independent of their primary sequences. Thus, the driving force of the transformation from the original to a disordered amyloid fold is expected to lie in the protein backbone common to all proteins. In order to investigate the thermodynamics of oligomerization, full geometry optimizations and frequency calculations were performed both on parallel and antiparallel β-pleated sheet model structures of [HCO–(Ala)1–6–NH2]2 and (For–Ala1–2–NH2)1–6peptides, both at the B3LYP and M05-2X/6-311++G(d,p)//M05-2X/6-31G(d) levels of theory, both in vacuum and in water. Our results show that relative entropy and enthalpy both show a hyperbolic decrease with increasing residue number and with increasing number of strands as well. Thus, di- and oligomerization are always thermodynamically favored. Antiparallel arrangements were found to have greater stability than parallel arrangements of the polypeptide backbones. During our study the relative changes in thermodynamic functions are found to be constant for long enough peptides, indicating that stability and entropy terms are predictable. All thermodynamic functions of antiparallel di- and oligomers show a staggered nature along the increasing residue number. By identifying and analyzing the 6 newly emerging dimer vibrational modes of the 10- and 14-membered building units, the staggered nature of the entropy function can be rationalized. Thus, the vanishing rotational and translational modes with respect to single strands are converted into entropy terms “holding tight” the dimers and oligomers formed, rationalizing the intrinsic adherence of natural polypeptide backbones to aggregate.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Royal Society of Chemistry
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Alzheimers Disease
dc.subject
Polymerization of Amyloid Peptides
dc.subject.classification
Otras Ciencias Químicas
dc.subject.classification
Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The role of entropy in initializing the aggregation of peptides: a first principle study on oligopeptide oligomerization
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-11-24T19:23:32Z
dc.journal.volume
14
dc.journal.number
4
dc.journal.pagination
1507-1516
dc.journal.pais
Reino Unido
dc.journal.ciudad
Cambridge
dc.description.fil
Fil: Pohl, Gábor. Eötvös Loránd University; Hungría
dc.description.fil
Fil: Jákli, Imre. Eötvös Loránd University; Hungría
dc.description.fil
Fil: Csizmadia, Imre G.. Eötvös Loránd University; Hungría
dc.description.fil
Fil: Papp, Dóra. Eötvös Loránd University; Hungría
dc.description.fil
Fil: Garibotto, Francisco Matías. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
dc.description.fil
Fil: Perczel, András. Eötvös Loránd University; Hungría
dc.journal.title
Physical Chemistry Chemical Physics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2012/CP/C2CP22821A#!divAbstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/ 10.1039/c2cp22821a
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