Cephalosporin-3'-diazeniumdiolates: targeted no-donor prodrugs for dispersing bacterial biofilms

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dc.contributor.authorBarraud, Nen_AU
dc.contributor.authorKardak, BGen_AU
dc.contributor.authorYepuri, NRen_AU
dc.contributor.authorHowlin, RPen_AU
dc.contributor.authorWebb, JSen_AU
dc.contributor.authorFaust, SNen_AU
dc.contributor.authorKjelleberg, Sen_AU
dc.contributor.authorRice, SAen_AU
dc.contributor.authorKelso, MJen_AU
dc.date.accessioned2014-03-31T21:53:37Zen_AU
dc.date.available2014-03-31T21:53:37Zen_AU
dc.date.issued2012-01-01en_AU
dc.date.statistics2014-04-01en_AU
dc.description.abstractCereal starch granules with high (>50%) amylose content are a promising source of nutritionally desirable resistant starch, i.e. starch that escapes digestion in the small intestine, but the structural features responsible are not fully understood. We report the effects of partial enzyme digestion of maize starch granules on amylopectin branch length profiles, double and single helix contents, gelatinisation properties, crystallinity and lamellar periodicity. Comparing results for three maize starches (27, 57, and 84% amylose) that differ in both structural features and amylase-sensitivity allows conclusions to be drawn concerning the rate-determining features operating under the digestion conditions used. All starches are found to be digested by a side-by-side mechanism in which there is no major preference during enzyme attack for amylopectin branch lengths, helix form, crystallinity or lamellar organisation. We conclude that the major factor controlling enzyme susceptibility is granule architecture, with shorter length scales not playing a major role as inferred from the largely invariant nature of numerous structural measures during the digestion process (XRD, NMR, SAXS, DSC, FACE). Results are consistent with digestion rates being controlled by restricted diffusion of enzymes within densely packed granular structures, with an effective surface area for enzyme attack determined by external dimensions (57 or 84% amylose - relatively slow) or internal channels and pores (27% amylose - relatively fast). Although the process of granule digestion is to a first approximation non-discriminatory with respect to structure at molecular and mesoscopic length scales, secondary effects noted include (i) partial crystallisation of V-type helices during digestion of 27% amylose starch, (ii) preferential hydrolysis of long amylopectin branches during the early stage hydrolysis of 27% and 57% but not 84% amylose starches, linked with disruption of lamellar repeating structure and (iii) partial B-type recrystallisation after prolonged enzyme incubation for 57% and 84% amylose starches but not 27% amylose starch. © 2012, Wiley-VCH Verlag GmbH & Co. KGaAen_AU
dc.identifier.citationBarraud, N., Kardak, B. G., Yepuri, N. R., Howlin, R. P., Webb, J. S., Faust, S. N., Kjelleberg, S., Rice, S. A., & Kelso, M. J. (2012). Cephalosporin-3'-diazeniumdiolates: targeted no-donor prodrugs for dispersing bacterial biofilms. Angewandte Chemie International Edition, 51(36), 9057-9060. doi:10.1002/anie.201202414en_AU
dc.identifier.govdoc4611en_AU
dc.identifier.issn1433-7851en_AU
dc.identifier.issue36en_AU
dc.identifier.journaltitleAngewandte Chemie International Editionen_AU
dc.identifier.pagination9057-9060en_AU
dc.identifier.urihttp://dx.doi.org/10.1002/anie.201202414en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/5360en_AU
dc.identifier.volume51en_AU
dc.language.isoenen_AU
dc.publisherWiley-V C H Verlag GMBHen_AU
dc.subjectAntibioticsen_AU
dc.subjectNitric oxideen_AU
dc.subjectPseudomonasen_AU
dc.subjectBacteriaen_AU
dc.subjectHydrolysisen_AU
dc.subjectMaizeen_AU
dc.titleCephalosporin-3'-diazeniumdiolates: targeted no-donor prodrugs for dispersing bacterial biofilmsen_AU
dc.typeJournal Articleen_AU
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