%0 Journal Article %1 RN262 %A Vera, A.M. %A Carcamo, J.J. %A Aliaga, A.E. %A Gomez-Jeria, J.S. %A Kogan, M.J. %A Campos-Vallette, M.M. %D 2015 %I 2014 Elsevier B.V. %J Spectrochimica Acta Part a-Molecular and Biomolecular Spectroscopy %K alzheimer-disease, anti-aggregation approximations, assemblies, beta-amyloid, calculations, clpffd dqcauchile extended hartree-fock htickel molecular-orbital nanoparticles, of peptide peptide, protein, sers, silver, spectroscopy, stability theories, theory type, %P 251-256 %R 10.1016/j.saa.2014.06.116 %T Interaction of the Clpffd Peptide with Gold Nanospheres. A Raman, Surface Enhanced Raman Scattering and Theoretical Study %U /brokenurl#<Go to ISI>://WOS:000342718700034 %V 134 %X In a previous work we demonstrated that toxic aggregates of the protein beta-amyloid (ATA beta) involved in the Alzheimer's disease (AD) can be destabilized upon electromagnetic irradiation of the peptide Cys-Leu-Pro-Phe-Phe-Asp (CLPFFD) adsorbed on gold nanospheres (AuNSs). For a selective recognition of the therapeutic target (i.e. ATA beta) of AD by the conjugates peptide-nanoparticle it is relevant to understand how the interaction between attached ligands and nanoparticles occurs. In this work a surface enhanced Raman scattering spectroscopy (SERS) study of the interactions of CLPFFD with AuNSs of 10 nm average diameter was carried out. The SERS data suggest that phenylalanine displays its aromatic ring coplanar to the surface which is supported by theoretical data obtained from molecular mechanics (MM) and Extended Huckel Theory (EHT) calculations.

@article{RN262, abstract = {In a previous work we demonstrated that toxic aggregates of the protein beta-amyloid (ATA beta) involved in the Alzheimer's disease (AD) can be destabilized upon electromagnetic irradiation of the peptide Cys-Leu-Pro-Phe-Phe-Asp (CLPFFD) adsorbed on gold nanospheres (AuNSs). For a selective recognition of the therapeutic target (i.e. ATA beta) of AD by the conjugates peptide-nanoparticle it is relevant to understand how the interaction between attached ligands and nanoparticles occurs. In this work a surface enhanced Raman scattering spectroscopy (SERS) study of the interactions of CLPFFD with AuNSs of 10 nm average diameter was carried out. The SERS data suggest that phenylalanine displays its aromatic ring coplanar to the surface which is supported by theoretical data obtained from molecular mechanics (MM) and Extended Huckel Theory (EHT) calculations. }, added-at = {2019-12-04T03:57:35.000+0100}, author = {Vera, A.M. and Carcamo, J.J. and Aliaga, A.E. and Gomez-Jeria, J.S. and Kogan, M.J. and Campos-Vallette, M.M.}, biburl = {https://www.bibsonomy.org/bibtex/2d4f53479681a3b7d82fddc014a0f724c/dqcauchile}, doi = {10.1016/j.saa.2014.06.116}, interhash = {6e7fa800085f70ea051bf5445e902183}, intrahash = {d4f53479681a3b7d82fddc014a0f724c}, issn = {1386-1425}, journal = {Spectrochimica Acta Part a-Molecular and Biomolecular Spectroscopy}, keywords = {alzheimer-disease, anti-aggregation approximations, assemblies, beta-amyloid, calculations, clpffd dqcauchile extended hartree-fock htickel molecular-orbital nanoparticles, of peptide peptide, protein, sers, silver, spectroscopy, stability theories, theory type,}, pages = {251-256}, publisher = {2014 Elsevier B.V.}, timestamp = {2019-12-04T03:58:17.000+0100}, title = {Interaction of the Clpffd Peptide with Gold Nanospheres. A Raman, Surface Enhanced Raman Scattering and Theoretical Study}, type = {Journal Article}, url = {/brokenurl#<Go to ISI>://WOS:000342718700034}, volume = 134, year = 2015 }