Multivariate design, synthesis, and biological evaluation of peptide inhibitors of FimC/FimH protein-protein interactions in uropathogenic Escherichia coli

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Fältnamn	Indikatorer	Metadata
000		02893naa a2200361 4500
001		oai:DiVA.org:umu-13553
003		SwePub
008		070511s2005 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-135532 URI
024	7	a https://doi.org/10.1021/jm040818l2 DOI
040		a (SwePub)umu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Larsson, Andreasu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)anslan95
245	1 0	a Multivariate design, synthesis, and biological evaluation of peptide inhibitors of FimC/FimH protein-protein interactions in uropathogenic Escherichia coli
264		c 2005-02-01
264	1	b American Chemical Society (ACS),c 2005
338		a print2 rdacarrier
520		a A peptide library targeting protein-protein interactions crucial for pilus assembly in Gram negative bacteria has been designed using statistical molecular design. A nonamer peptide scaffold was used, with seven positions being varied. The selection was performed in the building block space, and previously known structure-activity data were included in the design procedure. This resulted in a heavily reduced library consisting of 32 peptides which was prepared by solid-phase synthesis. The ability of the peptides to inhibit the protein-protein interaction between the periplasmic chaperone FimC and the pilus adhesin FimH was then determined in an ELISA. Novel peptides with the capability to inhibit the FimC/FimH protein(-)protein interaction to the same extent as the native FimC peptides were discovered. Multivariate QSAR studies of the response in the ELISA gave valuable information on the properties of amino acids which were preferred at the seven positions in the nonamer scaffold. This information can be used in attempts to develop optimized peptides and peptidomimetics that inhibit pilus assembly in pathogenic bacteria.
650	7	a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe
650	7	a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng
700	1	a Johansson, Susanne M. C.u Umeå universitet,Kemiska institutionen4 aut
700	1	a Pinkner, Jerome S.4 aut
700	1	a Hultgren, Scott J.4 aut
700	1	a Almqvist, Fredriku Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)fral0001
700	1	a Kihlberg, Janu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)jaki0001
700	1	a Linusson, Annau Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)analin99
710	2	a Umeå universitetb Kemiska institutionen4 org
773	0	t Journal of Medicinal Chemistryd : American Chemical Society (ACS)g 48:4, s. 935-945q 48:4<935-945x 0022-2623x 1520-4804
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-13553
856	4 8	u https://doi.org/10.1021/jm040818l

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Av författaren/redakt...: Larsson, Andreas; Johansson, Susan ...; Pinkner, Jerome ...; Hultgren, Scott ...; Almqvist, Fredri ...; Kihlberg, Jan; visa fler...; Linusson, Anna; visa färre...

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Av lärosätet: Umeå universitet

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