Krishna Prasad, K. ; Verma, Sandeep (2006) Ordering in a glycine-rich peptide conjugate: microscopic, fluorescence, and metalation studies Biopolymers, 83 (3). pp. 289-296. ISSN 0006-3525
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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/bip.205...
Related URL: http://dx.doi.org/10.1002/bip.20562
Abstract
Glycine residues play an intriguing role in peptide/protein structure where they can act as tightly packing amino acids with flexible bond angles. For example, structural role of glycines is highlighted in natural silk fibers where different structural polymorphs have been reported. This study deals with a glycine-rich segment from the conserved octarepeat (PHGGGWGQ) in prion protein. We have synthesized a bis-conjugate 3, containing a truncated pentapeptide segment (GGGWG), to study its time-dependent solution phase aggregation by a combination of microscopic methods and fluorescence. This discontinuous peptide conjugate 3 exhibited interesting photophysical properties upon self-assembly allowing us to propose a possible model of peptide filament formation. Taking note of the fact that prion octarepeats bind copper, we also demonstrate the ability of this conjugate to bind copper and the growth and ultrastructure of metallized fibers formed upon incubation. Enforcing peptide fiber formation in metal binding motifs offers an entry into metal impregnated fibers for possible nanobiotechnological applications.
Item Type: | Article |
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Source: | Copyright of this article belongs to John Wiley and Sons. |
Keywords: | Peptide; Self-assembly; Aggregation; Fluorescence; Microscopy |
ID Code: | 66213 |
Deposited On: | 21 Oct 2011 09:45 |
Last Modified: | 21 Oct 2011 09:45 |
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