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dc.contributor.author Khan, T.
dc.contributor.author Kaderbhai, Naheed N.
dc.contributor.author Kaderbhai, Mustak A.
dc.date.accessioned 2009-05-21T13:47:37Z
dc.date.available 2009-05-21T13:47:37Z
dc.date.issued 2008-06-01
dc.identifier.citation Khan , T , Kaderbhai , N N & Kaderbhai , M A 2008 , ' An anti-microbial peptide derivative of flesh fruit fly mimics secretory signal sequence and inhibits signal peptidase-I in the export pathway ' International Journal of Peptide Research and Therapeutics , vol 14 , no. 2 , pp. 173-181 . , 10.1007/s10989-008-9128-1 en
dc.identifier.other PURE: 103494
dc.identifier.other dspace: 2160/2350
dc.identifier.uri http://hdl.handle.net/2160/2350
dc.description Kaderbhai, N., Khan, T., Kaderbhai, M. A (2008). An anti-microbial peptide derivative of flesh fruit fly mimics secretory signal sequence and inhibits signal peptidase-I in the export pathway. International Journal of Peptide Research and Therapeutics, 14, (2), pp. 173-181 Keywords: Antimicrobial peptides - Signal peptidase-I - Signal sequence - Protein secretion IMPF: 01.08 Sponsorship: Wales Research and Innovation: R & D Systems en
dc.description.abstract Combinatorial search of the antimicrobial peptide R7SLCLLHCRLK from flesh fruit fly yielded a substantially more active peptide of the sequence KLKL5KLK-NH2 that had signal sequence character as revealed by Neural-network survey. Bioinformatics survey of KLKLnKLK revealed a sigmoidal relationship between SSP and the intervening Leu stretch. Synthetic enantiomeric KLKLnKLK peptides inhibited Escherichia coli signal peptidase-I, in vitro, in correlation with their SSPs; KLKL6(7)KLK exterted maximum inhibition. Both (l)-and (d)-forms were bactericidal to Gram-positive and Gram-negative bacteria. However, the protease-resistant (d)-KLKL6KLK-NH2 proved more potent than (d)-KLKL6KLK-NH2 at inhibiting the bacterial protein secretion prior to inducing bacterial lysis. Kinetic analyses of the interaction of these peptides with the signal peptidase-I revealed competitive inhibition with Ki of 10 μM and 35 μM for the (d)- and (l)-forms, respectively. The left and right-handed helicity of the respective peptides assessed by CD concurs with their probable interaction at the active site of signal peptidase-I. en
dc.format.extent 9 en
dc.language.iso eng
dc.relation.ispartof International Journal of Peptide Research and Therapeutics en
dc.subject Antimicrobial peptides en
dc.subject Signal peptidase-I en
dc.subject Signal sequence en
dc.subject Protein secretion en
dc.title An anti-microbial peptide derivative of flesh fruit fly mimics secretory signal sequence and inhibits signal peptidase-I in the export pathway en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1007/s10989-008-9128-1
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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