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A backbone-reversed all-beta polypeptide (retro-CspA) folds and assembles into amyloid nanofibres.

IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh


Field	Value

Title	A backbone-reversed all-beta polypeptide (retro-CspA) folds and assembles into amyloid nanofibres.

Creator	Shukla, Anshuman Raje, Manoj Guptasarma, Purnananda

Subject	QR Microbiology

Description	The backbone-reversed or 'retro', form of a model all-beta-sheet protein, Escherichia coli CspA, was produced from a synthetic gene in E.coli in fusion with an N-terminal affinity tag. Following purification under denaturing conditions and dialysis-based removal of urea, the protein was found to fold into a soluble, poorly structured multimer. Upon concentration, this state readily transformed into amyloid nanofibres. Congo Red-binding amorphous forms were also observed. Since a beta-sheet-forming sequence is expected to retain high beta-sheet-forming propensity even after backbone reversal and given the fact that folding of retro-CspA occurs only to a poorly structured form, we conclude that the increase effected in protein concentration may be responsible for the formation of intermolecular beta-sheets, facilitating the bleeding away of the protein's conformational equilibrium into aggregates that generate well-formed fibres. Since every molecule in these fibres contains a peptide tag for binding Ni(2+), the fibres may provide a template for deposition of nickel to generate novel materials.

Publisher	Oxford University Press

Date	2003-12

Type	Article PeerReviewed

Format	application/pdf

Identifier	http://crdd.osdd.net/open/221/1/guptasarma2003.2.pdf Shukla, Anshuman and Raje, Manoj and Guptasarma, Purnananda (2003) A backbone-reversed all-beta polypeptide (retro-CspA) folds and assembles into amyloid nanofibres. Protein engineering, 16 (12). pp. 875-9. ISSN 0269-2139

Relation	http://peds.oxfordjournals.org/content/16/12/875.long http://crdd.osdd.net/open/221/