Ordered self-assembly of a glycine-rich linear and cyclic hexapeptide: contrasting ultrastructural morphologies of fiber growth

Joshi, K. B. ; Verma, Sandeep (2006) Ordered self-assembly of a glycine-rich linear and cyclic hexapeptide: contrasting ultrastructural morphologies of fiber growth Supramolecular Chemistry, 18 (5). pp. 405-414. ISSN 1061-0278

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Official URL: http://www.tandfonline.com/doi/abs/10.1080/1061580...

Related URL: http://dx.doi.org/10.1080/10615800600658875

Abstract

Self-assembly is a widely occurring phenomenon in chemistry and biology, where nanoscopic building blocks are organized to yield well-defined aggregates and supramolecular structures. One such example is ordered protein aggregation, which is primarily driven by hydrogen bonding, hydrophobic interactions and other non-covalent stabilizing factors. This report describes differing ultrastructural morphologies of a cyclic and linear hexapeptide, possessing the same amino acid sequence. Microscopic studies reveal two dissimilar pathways leading to self-assembly: one with spherical pre-fibrillar intermediate, while another one displaying spherulite-like "Maltese-cross" patterns. Detailed analysis provides crucial insight into initiation, propagation and growth of peptide fibers in two constructs.

Item Type:Article
Source:Copyright of this article belongs to Taylor and Francis Group.
Keywords:Peptide; Aggregation; Self-assembly; Conjugate; Ultrastructure
ID Code:66256
Deposited On:21 Oct 2011 09:45
Last Modified:21 Oct 2011 09:45

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