Nanofibers Formed Through pi ... pi Stacking of the Complexes of Glucosyl-C2-salicyl-imine and Phenylalanine: Characterization by Microscopy, Modeling by Molecular Mechanics, and Interaction by alpha-Helical and beta-Sheet Proteins
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Title |
Nanofibers Formed Through pi ... pi Stacking of the Complexes of Glucosyl-C2-salicyl-imine and Phenylalanine: Characterization by Microscopy, Modeling by Molecular Mechanics, and Interaction by alpha-Helical and beta-Sheet Proteins
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Creator |
ACHARYA, A
RAMANUJAM, B MITRA, A RAO, CP |
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Subject |
peptide-amphiphile nanofibers
amyloid polypeptide iapp self-assembling peptide selective recognition amino-acids fluorescence derivatives binding oligonucleotide nanostructures 1-(d-glucopyranosyl-2 '-deoxy-2 '-iminomethyl)-2-hydroxy-benzene amphiphile nanofibers pi ... pi interactions maldi microscopy molecular mechanics (mm plus ) alpha-helical albumins beta-sheet lectins |
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Description |
This paper deals with the self-assembly of the 1:1 complex of two different amphiphiles, namely, a glucosyl-salicyl-imino conjugate (L) and phenylalanine (Phe), forming nanofibers over a period of time through pi ... pi interactions. Significant enhancement observed in the fluorescence intensity of L at similar to 423 nm band and the significant decrease observed in the absorbance of the similar to 215 nm band are some characteristics of this self-assembly. Matrix-assisted laser desorption ionization/time of flight titration carried out at different time intervals supports the formation of higher aggregates. Atomic force microscopy (AIM), transmission electron microscopy, and scanning electron miscroscopy results showed the formation of nanofibers for the solutions of L with phenylalanine. In dynamic light scattering measurements, the distribution of the particles extends to a higher diameter range over time, indicating a slow kinetic process of assembly. Similar spectral and microscopy studies carried out with the control molecules support the role of the amino acid moiety over the simple - COOH moiety as well as the side chain phenyl moiety in association with the amino acid, in the formation of these fibers. All these observations support the presence of pi ... pi interactions between the initially formed 1:1 complexes leading to the fiber formation. The aggregation of 1:1 complexes leading to fibers followed by the formation of bundles has been modeled by molecular mechanics studies. Thus the fiber formation with L is limited to phenylalanine and not to any other naturally occurring amino acid and hence a polymer composed of two different biocompatible amphiphiles. AFM studies carried out between the fiber forming mixture and proteins resulted in the observation that only BSA selectively adheres to the fiber among the three alpha-helical and two beta-sheet proteins studied and hence may be of use in some medical applications.
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Publisher |
AMER CHEMICAL SOC
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Date |
2011-07-14T13:41:24Z
2011-12-26T12:48:24Z 2011-12-27T05:36:56Z 2011-07-14T13:41:24Z 2011-12-26T12:48:24Z 2011-12-27T05:36:56Z 2010 |
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Type |
Article
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Identifier |
ACS NANO, 4(7), 4061-4073
1936-0851 http://dx.doi.org/10.1021/nn1006286 http://dspace.library.iitb.ac.in/xmlui/handle/10054/3969 http://hdl.handle.net/10054/3969 |
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Language |
en
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